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Conserved domains on  [gi|697043810|ref|XP_009584666|]
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PREDICTED: outer dense fiber protein 2, partial [Fulmarus glacialis]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 60-279 1.29e-11

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  60 KTLKDEMN-KEIELARKQFQSQLAELEKLPEILKITETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMEMTRE 138
Cdd:COG1196  216 RELKEELKeLEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810 139 RYQSAQEEKKQLTLKVEELERKLETTSAQNIEFLQVIAKREESIHQCQLRLEEKTRECSSLARQLEMAIEDAKRQVEQTR 218
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697043810 219 ERAKSRERAAQSKmLDLETQLSRNKTELNQLRRSKDDAERRYESRLQDLKDRLEQSESTNR 279
Cdd:COG1196  376 EAEEELEELAEEL-LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 60-279 1.29e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  60 KTLKDEMN-KEIELARKQFQSQLAELEKLPEILKITETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMEMTRE 138
Cdd:COG1196  216 RELKEELKeLEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810 139 RYQSAQEEKKQLTLKVEELERKLETTSAQNIEFLQVIAKREESIHQCQLRLEEKTRECSSLARQLEMAIEDAKRQVEQTR 218
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697043810 219 ERAKSRERAAQSKmLDLETQLSRNKTELNQLRRSKDDAERRYESRLQDLKDRLEQSESTNR 279
Cdd:COG1196  376 EAEEELEELAEEL-LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-291 1.16e-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: 59.30  E-value: 1.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810    50 AKLEKCDKENKTLKDEMNKEIELARKQFQSQLAELEKLPEILKITETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQ 129
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   130 GDKMEMTRERYQSAQEEKKQLTLKVEELERKLETTSAQNIEFLQVIAKREESIHQCQLRLEEKTRECSSLARQLEMAIED 209
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   210 AKRQVEQTRERAKSRERAAQSkMLDLETQLSRNKTELNQL---RRSKDDAERRYESRLQDLKDRLEQSESTNRSMQNYVQ 286
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAE-IEELEELIEELESELEALlneRASLEEALALLRSELEELSEELRELESKRSELRRELE 918


                   ....*
gi 697043810   287 FLKSS 291
Cdd:TIGR02168  919 ELREK 923
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 94-275 2.55e-04

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 41.55  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   94 TETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMEMTRERYQSAQEEKKQLTLKVEELERKLETTSAQNIEFLQ 173
Cdd:pfam00261  13 AEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENRALKDEE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  174 VIAKREESIHQCQLRLEEKTRECSSLARQLEMaiedakrqVEQTRERAKSRERAAQSKMLDLETQLSRNKTELNQLRRSK 253
Cdd:pfam00261  93 KMEILEAQLKEAKEIAEEADRKYEEVARKLVV--------VEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASE 164

                         170       180
                  ....*....|....*....|....*
gi 697043810  254 DDA---ERRYESRLQDLKDRLEQSE 275
Cdd:pfam00261 165 EKAserEDKYEEQIRFLTEKLKEAE 189
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
63-277 2.64e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  63 KDEMNKEIELARKQFQSQLAELEKLPEILKitetQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMEMTRERYQ- 141
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERAE----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAe 548

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810 142 ---SAQEEKKQLTLKVEELERKLETTSAQNIEFLQVIAKRE--ESIHQCQLRLEEKTRECSSLARQLE--MAIEDAKR-Q 213
Cdd:PRK02224 549 leaEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslERIRTLLAAIADAEDEIERLREKREalAELNDERReR 628

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697043810 214 VEQTRERAK--------SRERAAQSKMLDLETQLSRNKTELNQLRRSKDDAERRYES------RLQDLKDRLEQSEST 277
Cdd:PRK02224 629 LAEKRERKReleaefdeARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAveneleELEELRERREALENR 706
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 60-279 1.29e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  60 KTLKDEMN-KEIELARKQFQSQLAELEKLPEILKITETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMEMTRE 138
Cdd:COG1196  216 RELKEELKeLEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810 139 RYQSAQEEKKQLTLKVEELERKLETTSAQNIEFLQVIAKREESIHQCQLRLEEKTRECSSLARQLEMAIEDAKRQVEQTR 218
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697043810 219 ERAKSRERAAQSKmLDLETQLSRNKTELNQLRRSKDDAERRYESRLQDLKDRLEQSESTNR 279
Cdd:COG1196  376 EAEEELEELAEEL-LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 32-282 2.51e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 2.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  32 ETYKSQVLKTQMEADDVAAKLEKCDKEnktlKDEMNKEIELARKQFQSQLAELEKLPEILKITETQLAECQDQLQSYEKK 111
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAE----LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810 112 NVDLSAMIADLRQLIELQGDKMEMTRERYQSAQEEKKQLTLKVEELERKLETTSAQNIEFLQVIAKREESIHQCQLRLEE 191
Cdd:COG1196  311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810 192 KTRECSSLARQLEmAIEDAKRQVEQTRERAKSRERAAQSKMLDLETQLSRNKTELNQLRRSKDDAERRYESRLQDLKDRL 271
Cdd:COG1196  391 ALRAAAELAAQLE-ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                        250
                 ....*....|.
gi 697043810 272 EQSESTNRSMQ 282
Cdd:COG1196  470 EEAALLEAALA 480
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-291 1.16e-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: 59.30  E-value: 1.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810    50 AKLEKCDKENKTLKDEMNKEIELARKQFQSQLAELEKLPEILKITETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQ 129
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   130 GDKMEMTRERYQSAQEEKKQLTLKVEELERKLETTSAQNIEFLQVIAKREESIHQCQLRLEEKTRECSSLARQLEMAIED 209
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   210 AKRQVEQTRERAKSRERAAQSkMLDLETQLSRNKTELNQL---RRSKDDAERRYESRLQDLKDRLEQSESTNRSMQNYVQ 286
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAE-IEELEELIEELESELEALlneRASLEEALALLRSELEELSEELRELESKRSELRRELE 918


                   ....*
gi 697043810   287 FLKSS 291
Cdd:TIGR02168  919 ELREK 923
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-226 1.54e-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: 58.91  E-value: 1.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810     3 MVPMEEKLNQAQMEVQQLKSSVRNYEGLVETYK---SQVLKTQMEADDVAAKLEKCDKENKTLKDEMNKEIELARKQFQS 79
Cdd:TIGR02168  276 VSELEEEIEELQKELYALANEISRLEQQKQILRerlANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810    80 QLAELEKLPEILKITETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMEMTRERYQSAQEEKKQLTLKVEELER 159
Cdd:TIGR02168  356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   160 KlettsaqniEFLQVIAKREESIHQCQLRLEEKTRECSSLA---RQLEMAIEDAKRQVEQTRERAKSRER 226
Cdd:TIGR02168  436 K---------ELQAELEELEEELEELQEELERLEEALEELReelEEAEQALDAAERELAQLQARLDSLER 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 16-285 4.65e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.30  E-value: 4.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810    16 EVQQLKSSVRNYEGLVETYKSQVLKTQMEADDVAAKLEKCDKENKTLKDEMNKEIELARKQFQSQLAEL----EKLPEIL 91
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELeaeiASLERSI 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810    92 KITETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMEMTRERYQSAQEEKKQLTLKVEELERKLETT---SAQN 168
Cdd:TIGR02169  311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETrdeLKDY 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   169 IEFLQVIAKREESIHQCQLRLEEKTRECSSLARQLEMAIEDAKRQVEQTRERAKSreraAQSKMLDLETQLSRNKTELNQ 248
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED----KALEIKKQEWKLEQLAADLSK 466

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 697043810   249 LRRSKDDAE---RRYESRLQDLKDRLEQSESTNRSMQNYV 285
Cdd:TIGR02169  467 YEQELYDLKeeyDRVEKELSKLQRELAEAEAQARASEERV 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 32-290 1.82e-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: 52.75  E-value: 1.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810    32 ETYKSQVLKTQMEADDVAAKLEKCDKENKTLKD---EMNKEIELARKQFQSQLAELEKLpeilkitETQLAECQDQLQSY 108
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELRLevsELEEEIEELQKELYALANEISRL-------EQQKQILRERLANL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   109 EKKNVDLSAMIADLRQlielqgdkmemtreRYQSAQEEKKQLTLKVEELERKLETTSAQNIEFLQVIAKREESIHQCQLR 188
Cdd:TIGR02168  315 ERQLEELEAQLEELES--------------KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   189 LEEKTRECSSLARQLEMA----------IEDAKRQVEQTRERAKSRERAAQS-KMLDLETQLSRNKTELNQLRRSKDDAE 257
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLnneierlearLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLE 460

                          250       260       270
                   ....*....|....*....|....*....|...
gi 697043810   258 RRYESrlqdLKDRLEQSESTNRSMQNYVQFLKS 290
Cdd:TIGR02168  461 EALEE----LREELEEAEQALDAAERELAQLQA 489
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 82-288 2.87e-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: 51.98  E-value: 2.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810    82 AELEKLPEILKITETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMEMTRERYQSAQEEKKQLTLKVEELERKL 161
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   162 EttsaqniEFLQVIAKREESIHQcqlrLEEKTRECSSLARQLEMAIEDAKRQVEQTRERAKSRERAAQskmlDLETQLSR 241
Cdd:TIGR02168  757 T-------ELEAEIEELEERLEE----AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT----LLNEEAAN 821

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 697043810   242 NKTELNQLRRSKDDAERRYESRLQDLKDRLEQSESTNRSMQNYVQFL 288
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 79-298 1.47e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 1.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810    79 SQLAELEKLPEILKITETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMEMTRERYQSAQEEKKQLTLKVEELE 158
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   159 RKLETTSAQNIEFLQVIAKREESIHQCQLRLEE-KTRECSSLARQLEMAIEDAKRQVEQTRERAKSRERAAQSKMLDLEt 237
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE- 829

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697043810   238 QLSRNKTELNQLRRSKDDAERRYESRLQDLKDRLEQSESTNRSMQNYVQFLKSSYANVFGE 298
Cdd:TIGR02169  830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 45-278 2.10e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.61  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  45 ADDVAAKLEKCDKENKTLKDEMNKEIELARKQFQSQLAELEKLPEILKITETQLAECQDQLQSYEKKNVDLSAMIADLRQ 124
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810 125 LIELQGDKM-EMTRERYQSAQEEKKQLTLKVEELERKLETTSAQNiEFLQVIAKREESIHQCQLRLEEKTRECSSLARQL 203
Cdd:COG4942   98 ELEAQKEELaELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAELEAERAEL 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697043810 204 emaiEDAKRQVEQTRERAKSRERAAQSKMLDLETQLSRNKTELNQLRRSKDDAERRYESRLQDLKDRLEQSESTN 278
Cdd:COG4942  177 ----EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-241 8.73e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 8.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   7 EEKLNQAQMEVQQLKSSVRNYEGLVETYKSQVLKTQMEADDVAAKLEKCDKENKTLKdemnKEIELARKQFQSQLAELEK 86
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE----EELEELEEELEELEEELEE 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  87 LPEILKITETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMEMTRERYQSAQEEKKQLTLKVEELERKLETTSA 166
Cdd:COG1196  349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697043810 167 QNIEFLQVIAKREESIHQCQLRLEEKTRECSSLARQLEMAIEDAKRQVEQTRERAKSRERAAQSKMLDLETQLSR 241
Cdd:COG1196  429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
64-273 2.14e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   64 DEMNKEIELARKQfQSQLAELEKLPEILKITETQLAECQDQLQSYEKKNvdLSAMIADLRQLIELQGDKMEMTRERYQSA 143
Cdd:COG4913   238 ERAHEALEDAREQ-IELLEPIRELAERYAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARLEAELERL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  144 QEEKKQLTLKVEELERKLETTSAQNIEFLqviakrEESIHQCQLRLEEKTRECSSLARQLEM----------AIEDAKRQ 213
Cdd:COG4913   315 EARLDALREELDELEAQIRGNGGDRLEQL------EREIERLERELEERERRRARLEALLAAlglplpasaeEFAALRAE 388

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697043810  214 VEQTRERAKSRERAAQSKMLDLETQLSRNK-------TELNQLRRSKDdaerRYESRLQDLKDRLEQ 273
Cdd:COG4913   389 AAALLEALEEELEALEEALAEAEAALRDLRrelreleAEIASLERRKS----NIPARLLALRDALAE 451
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
91-273 3.87e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   91 LKITETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDkmemtRERYQSAQEEKKQLTLKVEELERKLETTSAQNIE 170
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-----LAEYSWDEIDVASAEREIAELEAELERLDASSDD 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  171 fLQVIAKREESIHQCQLRLEEKTRECSSLARQLEMAIEDAKRQVEQTRERAKSRERAAQSKM-LDLETQLSRNKTE--LN 247
Cdd:COG4913   687 -LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLEERFAAALGDavER 765

                         170       180
                  ....*....|....*....|....*.
gi 697043810  248 QLRRSKDDAERRYESRLQDLKDRLEQ 273
Cdd:COG4913   766 ELRENLEERIDALRARLNRAEEELER 791
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
67-288 6.34e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 6.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  67 NKEIELARKQFQSQLAELEKlpeilkitetQLAECQDQLQSYEKKNvdlsaMIADLRQLIELQGDKMEMTRERYQSAQEE 146
Cdd:COG3206  170 REEARKALEFLEEQLPELRK----------ELEEAEAALEEFRQKN-----GLVDLSEEAKLLLQQLSELESQLAEARAE 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810 147 KKQLTLKVEELERKLETTSAQNIEFLQ--VIAKREESIHQCQLRLEEKT--------------RECSSLARQLEMAIEDA 210
Cdd:COG3206  235 LAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSarytpnhpdvialrAQIAALRAQLQQEAQRI 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810 211 KRQVEQTRERAKSRERAAQSKMLDLETQ---LSRNKTELNQLRRSKDDAERRYESrlqdLKDRLEQSESTNRSMQNYVQF 287
Cdd:COG3206  315 LASLEAELEALQAREASLQAQLAQLEARlaeLPELEAELRRLEREVEVARELYES----LLQRLEEARLAEALTVGNVRV 390


                 .
gi 697043810 288 L 288
Cdd:COG3206  391 I 391
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 94-275 2.55e-04

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 41.55  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   94 TETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMEMTRERYQSAQEEKKQLTLKVEELERKLETTSAQNIEFLQ 173
Cdd:pfam00261  13 AEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENRALKDEE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  174 VIAKREESIHQCQLRLEEKTRECSSLARQLEMaiedakrqVEQTRERAKSRERAAQSKMLDLETQLSRNKTELNQLRRSK 253
Cdd:pfam00261  93 KMEILEAQLKEAKEIAEEADRKYEEVARKLVV--------VEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASE 164

                         170       180
                  ....*....|....*....|....*
gi 697043810  254 DDA---ERRYESRLQDLKDRLEQSE 275
Cdd:pfam00261 165 EKAserEDKYEEQIRFLTEKLKEAE 189
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
75-261 3.26e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  75 KQFQSQLAELEKLPEILKITETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDkmemtRERYQSAQEEKKQLTLKV 154
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-----YQELEALEAELAELPERL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810 155 EELERKLETTSaqniEFLQVIAKREESIHQCQLRLEEKTRECSSLARQlemAIEDAKRQVEQTRERAKSRERAAQSKMLD 234
Cdd:COG4717  149 EELEERLEELR----ELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEE 221

                        170       180
                 ....*....|....*....|....*..
gi 697043810 235 LEtQLSRNKTELNQLRRSKDDAERRYE 261
Cdd:COG4717  222 LE-ELEEELEQLENELEAAALEERLKE 247
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 17-292 4.55e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.96  E-value: 4.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810    17 VQQLKSSVRNYEGLVETYKSQVLKTQMEADDVAAKLEKcdkeNKTLKDEMNKEIELARKQFQSQLAELEKLPEILKITET 96
Cdd:TIGR00606  697 ISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPG----RQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810    97 QLAECQDQLQSYEKKNVDLSAMIADLRQLIELQgDKMEMTRERYQSAQEEK--KQLTLKVEELERKLETTSAQNIEFLQV 174
Cdd:TIGR00606  773 LLGTIMPEEESAKVCLTDVTIMERFQMELKDVE-RKIAQQAAKLQGSDLDRtvQQVNQEKQEKQHELDTVVSKIELNRKL 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   175 IAKREESIHQCQLRLEEKTRECSSLARQLEMAIEDAKRQVEQTRERAKSRERAAQSK--MLDLETQLSRNKTELNQLRRS 252
Cdd:TIGR00606  852 IQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKeqDSPLETFLEKDQQEKEELISS 931

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 697043810   253 KDDAERRYESRLQDLKDRLEQSESTNRSMQNYVQFLKSSY 292
Cdd:TIGR00606  932 KETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDY 971
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 138-276 7.03e-04

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: 7.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810 138 ERYQSAQEEKKQL-----TLKVEELERKLETTSAQNIEFLQVIAKREESIHQCQLRLEEKTRECSSLARQLEMAIEDAkR 212
Cdd:COG1196  213 ERYRELKEELKELeaellLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE-Y 291

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697043810 213 QVEQTRERAKSRERAAQSKMLDLETQLSRNKTELNQLRRSKDDAERRYESRLQDLKDRLEQSES 276
Cdd:COG1196  292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 81-300 7.51e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 7.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810    81 LAELEKLPEILKITETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMemtRERYQSAQEEKKQLTLKVEELERK 160
Cdd:TIGR02169  176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYEL---LKEKEALERQKEAIERQLASLEEE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   161 LETTSAQnieflqvIAKREESIHQCQLRLEEKTRECSSLARQLEMAIEDAKRQVEQTRERAKSRERAAQSKMLDLETQLS 240
Cdd:TIGR02169  253 LEKLTEE-------ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697043810   241 RNKTELNQLRRSKDDAERRYES---RLQDLKDRLEQSESTNRSMQNYVQFLKSSYANVFGESA 300
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELEREIEEerkRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-216 1.64e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810    7 EEKLNQAQMEVQQLKSSVRNYEGLVETYKSQ--VLKTQMEADDVAAKLEKCDKENKTLKdEMNKEIELARKQFQSQLAEL 84
Cdd:COG4913   630 EERLEALEAELDALQERREALQRLAEYSWDEidVASAEREIAELEAELERLDASSDDLA-ALEEQLEELEAELEELEEEL 708

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   85 EKLPEILKITETQLAECQDQLQSYEKKNVDLSAMIADLR------QLIELQGDKMEmtRERYQSAQEEKKQLTLKVEELE 158
Cdd:COG4913   709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELralleeRFAAALGDAVE--RELRENLEERIDALRARLNRAE 786

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  159 RKLE------------------TTSAQNIEFLQVIAK-REESIHQCQ-----LRLEEKTRECSSLARQLEMAIEDAKRQV 214
Cdd:COG4913   787 EELEramrafnrewpaetadldADLESLPEYLALLDRlEEDGLPEYEerfkeLLNENSIEFVADLLSKLRRAIREIKERI 866


                  ..
gi 697043810  215 EQ 216
Cdd:COG4913   867 DP 868
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 97-271 1.73e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  97 QLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMEMTRERYQSAQEEKKQLTLKVEELERKLETTSAQ-----NIEF 171
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrNNKE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810 172 LQVIAKREESIHQCQLRLEEKTREcsslarqLEMAIEDAKRQVEQTRERAKSRERAAQSKMLDLETQLSRNKTELNQLRR 251
Cdd:COG1579   91 YEALQKEIESLKRRISDLEDEILE-------LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163

                        170       180
                 ....*....|....*....|
gi 697043810 252 SKDDAERRYESRLQDLKDRL 271
Cdd:COG1579  164 EREELAAKIPPELLALYERI 183
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 7-226 1.86e-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: 39.75  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   7 EEKLNQAQMEVQQLKSSVRNYEGLVETYKSQVLKTQMEADDVAAKLEKCDKENKTLK---DEMNKEIELARKQFQSQLAE 83
Cdd:COG4942   33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEkeiAELRAELEAQKEELAELLRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  84 LEKLPEILKITEtqLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMEMTRERyQSAQEEKKQLTLKVEELERKLET 163
Cdd:COG4942  113 LYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR-AELEAERAELEALLAELEEERAA 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697043810 164 TSAQNIEFLQVIAKREESIHQCQLRLEEKTRECSSLARQLEMAIEDAKRQVEQTRERAKSRER 226
Cdd:COG4942  190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
63-277 2.64e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  63 KDEMNKEIELARKQFQSQLAELEKLPEILKitetQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMEMTRERYQ- 141
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERAE----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAe 548

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810 142 ---SAQEEKKQLTLKVEELERKLETTSAQNIEFLQVIAKRE--ESIHQCQLRLEEKTRECSSLARQLE--MAIEDAKR-Q 213
Cdd:PRK02224 549 leaEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslERIRTLLAAIADAEDEIERLREKREalAELNDERReR 628

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697043810 214 VEQTRERAK--------SRERAAQSKMLDLETQLSRNKTELNQLRRSKDDAERRYES------RLQDLKDRLEQSEST 277
Cdd:PRK02224 629 LAEKRERKReleaefdeARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAveneleELEELRERREALENR 706
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
131-273 3.13e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  131 DKMEMTRERYQSAQEEKKQLTLKVEELERKLETTSAQNIEFLQVIAKREEsihqcQLRLEEKTRECSSLARQLEMAIEDA 210
Cdd:COG4913   610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD-----EIDVASAEREIAELEAELERLDASS 684

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697043810  211 K--RQVEQTRERAKSRERAAQSKMLDLETQLSRNKTELNQLRRSKDDAERRYESRLQDLKDRLEQ 273
Cdd:COG4913   685 DdlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 12-230 4.07e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  12 QAQMEVQQLKSSVRNYEGLVETYKSQVLKTQMEADDVAAKLEKCDKENKTLKDEM---NKEIELARKQFQSQLAELEKLP 88
Cdd:COG3883   13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIdklQAEIAEAEAEIEERREELGERA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  89 EILKITETQLAECQDQLQSyeKKNVDLSAMIADLRQLIELQGDKMEMTRERYQSAQEEKKQLTLKVEELERKLETTSAQN 168
Cdd:COG3883   93 RALYRSGGSVSYLDVLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697043810 169 IEFLQVIAKREESIHQCQLRLEEKTRECSSLARQLEMAIEDAKRQVEQTRERAKSRERAAQS 230
Cdd:COG3883  171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-274 6.19e-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: 38.50  E-value: 6.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810     7 EEKLNQAQMEVQQLKSSVRNYEGLVETYKSQVLKTQMEADDVAAKLEKCDKENKTLKDEMNKEIELARKQfqsqLAELEK 86
Cdd:TIGR02168  802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL----ESELEA 877

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810    87 LPEILKITETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMEMTRERYQSAQEEKKQLTLKV-EELERKLEtts 165
Cdd:TIGR02168  878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLE--- 954

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   166 aqniEFLQVIAKREESIHQCQLRLEEKTRECSSLARQLEMAIEDAKRQVEQTRERAKSRERAAQSKmldletqlsrnkte 245
Cdd:TIGR02168  955 ----EAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAK-------------- 1016

                          250       260
                   ....*....|....*....|....*....
gi 697043810   246 lNQLRRSKDDAERRYESRLQDLKDRLEQS 274
Cdd:TIGR02168 1017 -ETLEEAIEEIDREARERFKDTFDQVNEN 1044
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 95-280 7.85e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.50  E-value: 7.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  95 ETQLAECQDQLQSYEKKNVDLSAMIADLRQLIELQGDKMEMTRERYQSAQEEKKQLTLKVEELERKLETTSAQNIEFLQV 174
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810 175 IAKREESIHQCQL------------------RLEEKTRECSSLARQLEMAIEDAKRQVEQTRERAKSRERAAQSKMLDLE 236
Cdd:COG3883   95 LYRSGGSVSYLDVllgsesfsdfldrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 697043810 237 TQLSRNKTELNQLRRSKDDAERRYESRLQDLKDRLEQSESTNRS 280
Cdd:COG3883  175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 7-273 8.29e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 37.85  E-value: 8.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810     7 EEKLNQAQMEVQQLKSSVRNYEGLVETYKSQVLKTQMEADDVAAKLEKCDKENKTLKDEMNKeIELARKQFQSQLAELEk 86
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK-LSKERKLLEERISEFT- 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810    87 lpeilkiteTQLAECQDQLQSYEKKNVDLSAMIADLrqliELQGDKMEMTRERYQSAqeeKKQLTLKVEELERKLETTSA 166
Cdd:pfam01576  166 ---------SNLAEEEEKAKSLSKLKNKHEAMISDL----EERLKKEEKGRQELEKA---KRKLEGESTDLQEQIAELQA 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   167 QNIEFLQVIAKREESIHQCQLRLEEKTRECSSLA---RQLEMAIEDAKRQVE---QTRERAKSRERAAQSKMLDLETQL- 239
Cdd:pfam01576  230 QIAELRAQLAKKEEELQAALARLEEETAQKNNALkkiRELEAQISELQEDLEserAARNKAEKQRRDLGEELEALKTELe 309

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 697043810   240 -------------SRNKTELNQLRRSKDDAERRYESRLQDLKDRLEQ 273
Cdd:pfam01576  310 dtldttaaqqelrSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQ 356
PRK06975 PRK06975
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
 42-136 8.41e-03

bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed


Pssm-ID: 235899 [Multi-domain]  Cd Length: 656  Bit Score: 37.78  E-value: 8.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  42 QMEADDVAAKLEKCDKENKTLKDEMNKEIELAR---KQFQSQLAELEklpeilkiteTQLAECQDQLQSYEKKNVDLSA- 117
Cdd:PRK06975 345 NRKVDRLDQELVQRQQANDAQTAELRVKTEQAQasvHQLDSQFAQLD----------GKLADAQSAQQALEQQYQDLSRn 414

                         90       100
                 ....*....|....*....|...
gi 697043810 118 ----MIADLRQLIELQGDKMEMT 136
Cdd:PRK06975 415 rddwMIAEVEQMLSSASQQLQLT 437
PTZ00121 PTZ00121
MAEBL; Provisional
 32-254 8.96e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 8.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810   32 ETYKSQVLKTQMEADDVAAKLEKCDKENKTLKDEMNKEIELARKQFQSQLAELEKLPEILKITETQLAECQDQLQSYEKK 111
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697043810  112 NVDLSAMIADLRQLIEL---------QGDKMEMTRERYQSAQEEKKQLTLKVEELERKLETTSAQNIEFLQVIAKREESI 182
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAkkkaeedkkKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA 1459

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697043810  183 HQCQLRLEEKtRECSSLARQLEMA--IEDAKRQVEQTRERAKSRERAAQSKMLDLETQLSRNKTELNQLRRSKD 254
Cdd:PTZ00121 1460 EEAKKKAEEA-KKADEAKKKAEEAkkADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
 
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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