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Conserved domains on  [gi|281427190|ref|NP_001163943|]
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cell cycle and apoptosis regulator protein 2 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DBC1 pfam14443
DBC1; DBC1 and it homologs from diverse eukaryotes are a catalytically inactive version of the ...
 340-457 3.71e-55

DBC1; DBC1 and it homologs from diverse eukaryotes are a catalytically inactive version of the Nudix hydrolase (MutT) domain. DBC1 is predicted to bind NAD metabolites and regulate the activity of SIRT1 or related deacetylases by sensing the soluble products or substrates of the NAD-dependent deacetylation reaction.


:

Pssm-ID: 464175  Cd Length: 123  Bit Score: 186.39  E-value: 3.71e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190  340 EHPLKQLKFLLG--RKEEEAVLVGGEWSPSLDGLDPQADPQVLVRTAIRCAQAQTGIDLSTCTKWWRFAEFQYLQP---G 414
Cdd:pfam14443   1 VHPCKLLKFLVGdrGKDNEIMAIGGPWSPSLDGADPTTDPSVLIRTAIRTTKALTGIDLSNCTQWYRFAEVHYYRPktdG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 281427190  415 PPRQLHTVVVYLPDVWTIMPTLEEWEALCQQKATEAAPQPQEA 457
Cdd:pfam14443  81 FPSRQEITVIFLPDVSSCLPSLEEWESLWLQYRKALLEKEREA 123
S1-like pfam14444
S1-like; S1-like RNA binding domain found in DBC1
 55-112 1.52e-32

S1-like; S1-like RNA binding domain found in DBC1


:

Pssm-ID: 464176  Cd Length: 58  Bit Score: 120.17  E-value: 1.52e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281427190   55 QRVFTGIVTSLHDYFGVVDEEVFFQLSVVKGRLPQLGEKVLVKAAYNPGQAVPWNAVK 112
Cdd:pfam14444   1 QRVFTGVVTKLQDYFGFVDEDVFFQLSVVKGRLPQVGDRVLVEAVYNPNMPFKWNAQR 58
BURAN pfam19257
BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.
 234-315 3.34e-17

BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.


:

Pssm-ID: 466013  Cd Length: 82  Bit Score: 76.97  E-value: 3.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190  234 DSPTCDFLELQRRYRSLLVPSDFLSVHLSWLSAFPLGQPFSLHHPSRIQVSSEKEAAPDTGAEPSPEDSDPTYSSKVLLL 313
Cdd:pfam19257   1 DSVERDYLELRKRYPRLYIPSDFSKLVLCWVETFPPLSPLPLDTPVSFHVMEKEVEPPLEQPAEAALEPADRYNAKVMLL 80


                  ..
gi 281427190  314 SS 315
Cdd:pfam19257  81 SG 82
LAIKA pfam19256
LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.
 511-559 7.96e-13

LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.


:

Pssm-ID: 466012 [Multi-domain]  Cd Length: 68  Bit Score: 64.19  E-value: 7.96e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 281427190  511 RPGCVNLSLYGIVEDRRP-KERISFEVVVLAELFVEMLQRDFGYRIYKVL 559
Cdd:pfam19256  19 KFDCKSLSLDGLLDYREDdTKESTFEVSLFAELFHEMLQRDFGFTIYKAL 68
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 813-917 3.51e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 3.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190   813 SLLQRAEQQDSGRLY----LENKIHTLELKLEESHNRFSATEVTNKTLAAEMQELRARLAEAEETARTVERQKNQLQRQM 888
Cdd:TIGR02168  719 KELEELSRQISALRKdlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798

                           90       100
                   ....*....|....*....|....*....
gi 281427190   889 QDFRRRLTPLHLEMQRIVEKADSWVEKEE 917
Cdd:TIGR02168  799 KALREALDELRAELTLLNEEAANLRERLE 827
 
Name Accession Description Interval E-value
DBC1 pfam14443
DBC1; DBC1 and it homologs from diverse eukaryotes are a catalytically inactive version of the ...
 340-457 3.71e-55

DBC1; DBC1 and it homologs from diverse eukaryotes are a catalytically inactive version of the Nudix hydrolase (MutT) domain. DBC1 is predicted to bind NAD metabolites and regulate the activity of SIRT1 or related deacetylases by sensing the soluble products or substrates of the NAD-dependent deacetylation reaction.


Pssm-ID: 464175  Cd Length: 123  Bit Score: 186.39  E-value: 3.71e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190  340 EHPLKQLKFLLG--RKEEEAVLVGGEWSPSLDGLDPQADPQVLVRTAIRCAQAQTGIDLSTCTKWWRFAEFQYLQP---G 414
Cdd:pfam14443   1 VHPCKLLKFLVGdrGKDNEIMAIGGPWSPSLDGADPTTDPSVLIRTAIRTTKALTGIDLSNCTQWYRFAEVHYYRPktdG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 281427190  415 PPRQLHTVVVYLPDVWTIMPTLEEWEALCQQKATEAAPQPQEA 457
Cdd:pfam14443  81 FPSRQEITVIFLPDVSSCLPSLEEWESLWLQYRKALLEKEREA 123
S1-like pfam14444
S1-like; S1-like RNA binding domain found in DBC1
 55-112 1.52e-32

S1-like; S1-like RNA binding domain found in DBC1


Pssm-ID: 464176  Cd Length: 58  Bit Score: 120.17  E-value: 1.52e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281427190   55 QRVFTGIVTSLHDYFGVVDEEVFFQLSVVKGRLPQLGEKVLVKAAYNPGQAVPWNAVK 112
Cdd:pfam14444   1 QRVFTGVVTKLQDYFGFVDEDVFFQLSVVKGRLPQVGDRVLVEAVYNPNMPFKWNAQR 58
BURAN pfam19257
BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.
 234-315 3.34e-17

BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.


Pssm-ID: 466013  Cd Length: 82  Bit Score: 76.97  E-value: 3.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190  234 DSPTCDFLELQRRYRSLLVPSDFLSVHLSWLSAFPLGQPFSLHHPSRIQVSSEKEAAPDTGAEPSPEDSDPTYSSKVLLL 313
Cdd:pfam19257   1 DSVERDYLELRKRYPRLYIPSDFSKLVLCWVETFPPLSPLPLDTPVSFHVMEKEVEPPLEQPAEAALEPADRYNAKVMLL 80


                  ..
gi 281427190  314 SS 315
Cdd:pfam19257  81 SG 82
LAIKA pfam19256
LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.
 511-559 7.96e-13

LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.


Pssm-ID: 466012 [Multi-domain]  Cd Length: 68  Bit Score: 64.19  E-value: 7.96e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 281427190  511 RPGCVNLSLYGIVEDRRP-KERISFEVVVLAELFVEMLQRDFGYRIYKVL 559
Cdd:pfam19256  19 KFDCKSLSLDGLLDYREDdTKESTFEVSLFAELFHEMLQRDFGFTIYKAL 68
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 813-917 3.51e-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: 41.20  E-value: 3.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190   813 SLLQRAEQQDSGRLY----LENKIHTLELKLEESHNRFSATEVTNKTLAAEMQELRARLAEAEETARTVERQKNQLQRQM 888
Cdd:TIGR02168  719 KELEELSRQISALRKdlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798

                           90       100
                   ....*....|....*....|....*....
gi 281427190   889 QDFRRRLTPLHLEMQRIVEKADSWVEKEE 917
Cdd:TIGR02168  799 KALREALDELRAELTLLNEEAANLRERLE 827
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
828-913 4.83e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190 828 LENKIHTLELKLEESHNRFS-ATEVTNKTLAAEMQELRARLAEAEETARTVERQKNQLQRQMQDFRRRLTPLHLEmQRIV 906
Cdd:COG4717  168 LEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLK 246


                 ....*..
gi 281427190 907 EKADSWV 913
Cdd:COG4717  247 EARLLLL 253
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 806-907 5.71e-03

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 40.05  E-value: 5.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190  806 GSLINVGSLLQRAE-QQDSGRLYLENKIHTLELKLEESHNRFSATEVTNktlaaemQELRARLAEAEETARTVERQKNQL 884
Cdd:pfam19220 216 GQLAAEQAERERAEaQLEEAVEAHRAERASLRMKLEALTARAAATEQLL-------AEARNQLRDRDEAIRAAERRLKEA 288

                          90       100
                  ....*....|....*....|...
gi 281427190  885 QRQMQDFRRRLTPLHLEMQRIVE 907
Cdd:pfam19220 289 SIERDTLERRLAGLEADLERRTQ 311
 
Name Accession Description Interval E-value
DBC1 pfam14443
DBC1; DBC1 and it homologs from diverse eukaryotes are a catalytically inactive version of the ...
 340-457 3.71e-55

DBC1; DBC1 and it homologs from diverse eukaryotes are a catalytically inactive version of the Nudix hydrolase (MutT) domain. DBC1 is predicted to bind NAD metabolites and regulate the activity of SIRT1 or related deacetylases by sensing the soluble products or substrates of the NAD-dependent deacetylation reaction.


Pssm-ID: 464175  Cd Length: 123  Bit Score: 186.39  E-value: 3.71e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190  340 EHPLKQLKFLLG--RKEEEAVLVGGEWSPSLDGLDPQADPQVLVRTAIRCAQAQTGIDLSTCTKWWRFAEFQYLQP---G 414
Cdd:pfam14443   1 VHPCKLLKFLVGdrGKDNEIMAIGGPWSPSLDGADPTTDPSVLIRTAIRTTKALTGIDLSNCTQWYRFAEVHYYRPktdG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 281427190  415 PPRQLHTVVVYLPDVWTIMPTLEEWEALCQQKATEAAPQPQEA 457
Cdd:pfam14443  81 FPSRQEITVIFLPDVSSCLPSLEEWESLWLQYRKALLEKEREA 123
S1-like pfam14444
S1-like; S1-like RNA binding domain found in DBC1
 55-112 1.52e-32

S1-like; S1-like RNA binding domain found in DBC1


Pssm-ID: 464176  Cd Length: 58  Bit Score: 120.17  E-value: 1.52e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281427190   55 QRVFTGIVTSLHDYFGVVDEEVFFQLSVVKGRLPQLGEKVLVKAAYNPGQAVPWNAVK 112
Cdd:pfam14444   1 QRVFTGVVTKLQDYFGFVDEDVFFQLSVVKGRLPQVGDRVLVEAVYNPNMPFKWNAQR 58
BURAN pfam19257
BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.
 234-315 3.34e-17

BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.


Pssm-ID: 466013  Cd Length: 82  Bit Score: 76.97  E-value: 3.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190  234 DSPTCDFLELQRRYRSLLVPSDFLSVHLSWLSAFPLGQPFSLHHPSRIQVSSEKEAAPDTGAEPSPEDSDPTYSSKVLLL 313
Cdd:pfam19257   1 DSVERDYLELRKRYPRLYIPSDFSKLVLCWVETFPPLSPLPLDTPVSFHVMEKEVEPPLEQPAEAALEPADRYNAKVMLL 80


                  ..
gi 281427190  314 SS 315
Cdd:pfam19257  81 SG 82
LAIKA pfam19256
LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.
 511-559 7.96e-13

LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.


Pssm-ID: 466012 [Multi-domain]  Cd Length: 68  Bit Score: 64.19  E-value: 7.96e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 281427190  511 RPGCVNLSLYGIVEDRRP-KERISFEVVVLAELFVEMLQRDFGYRIYKVL 559
Cdd:pfam19256  19 KFDCKSLSLDGLLDYREDdTKESTFEVSLFAELFHEMLQRDFGFTIYKAL 68
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 813-917 3.51e-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: 41.20  E-value: 3.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190   813 SLLQRAEQQDSGRLY----LENKIHTLELKLEESHNRFSATEVTNKTLAAEMQELRARLAEAEETARTVERQKNQLQRQM 888
Cdd:TIGR02168  719 KELEELSRQISALRKdlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798

                           90       100
                   ....*....|....*....|....*....
gi 281427190   889 QDFRRRLTPLHLEMQRIVEKADSWVEKEE 917
Cdd:TIGR02168  799 KALREALDELRAELTLLNEEAANLRERLE 827
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
828-913 4.83e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190 828 LENKIHTLELKLEESHNRFS-ATEVTNKTLAAEMQELRARLAEAEETARTVERQKNQLQRQMQDFRRRLTPLHLEmQRIV 906
Cdd:COG4717  168 LEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLK 246


                 ....*..
gi 281427190 907 EKADSWV 913
Cdd:COG4717  247 EARLLLL 253
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 828-917 5.70e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 5.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190 828 LENKIHTLELKLEESHNRFSATEVTNKTLAAEMQELRARLAEAEETARTVERQKNQLQRQMQDFRRRLTPLHLEMQRIVE 907
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                         90
                 ....*....|
gi 281427190 908 KADSWVEKEE 917
Cdd:COG1196  324 ELAELEEELE 333
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 806-907 5.71e-03

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 40.05  E-value: 5.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190  806 GSLINVGSLLQRAE-QQDSGRLYLENKIHTLELKLEESHNRFSATEVTNktlaaemQELRARLAEAEETARTVERQKNQL 884
Cdd:pfam19220 216 GQLAAEQAERERAEaQLEEAVEAHRAERASLRMKLEALTARAAATEQLL-------AEARNQLRDRDEAIRAAERRLKEA 288

                          90       100
                  ....*....|....*....|...
gi 281427190  885 QRQMQDFRRRLTPLHLEMQRIVE 907
Cdd:pfam19220 289 SIERDTLERRLAGLEADLERRTQ 311
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 804-908 7.25e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 38.07  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190  804 HNGSLINV-GSLLQRAEQQDSGRLYLENKIHTLELKLEESHNRFSATEVTNKTLAAEM-------QELRARLAEAEETAR 875
Cdd:pfam11559  32 NIARIINViYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELallqakeRQLEKKLKTLEQKLK 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 281427190  876 T----VERQKNQLQR----QMQDFRRRltplHLEMQRIVEK 908
Cdd:pfam11559 112 NekeeLQRLKNALQQiktqFAHEVKKR----DREIEKLKER 148
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 808-895 8.11e-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: 40.16  E-value: 8.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190   808 LINVGSLLQRAEQQDSgRLY-----LENKIH-TLELKLEESHNRFS-ATEVtnKTLAAEMQELRARLAEAEETARTVERQ 880
Cdd:pfam01576  442 LESVSSLLNEAEGKNI-KLSkdvssLESQLQdTQELLQEETRQKLNlSTRL--RQLEDERNSLQEQLEEEEEAKRNVERQ 518

                           90
                   ....*....|....*
gi 281427190   881 KNQLQRQMQDFRRRL 895
Cdd:pfam01576  519 LSTLQAQLSDMKKKL 533
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 805-911 8.99e-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: 8.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427190   805 NGSLIN-VGSLLQRAEQQDSGRLYLENKIHTLELKLEESHNRFSATEvtnktlaAEMQELRARLAEAEETARTVERQKNQ 883
Cdd:TIGR02168  651 DGDLVRpGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELE-------KALAELRKELEELEEELEQLRKELEE 723

                           90       100
                   ....*....|....*....|....*...
gi 281427190   884 LQRQMQDFRRRLTPLHLEMQRIVEKADS 911
Cdd:TIGR02168  724 LSRQISALRKDLARLEAEVEQLEERIAQ 751
 
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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