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Conserved domains on  [gi|556966607|ref|XP_005992646|]
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cell cycle and apoptosis regulator protein 2 isoform X1 [Latimeria chalumnae]

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 ...
 355-472 7.22e-58

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: 194.10  E-value: 7.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607  355 QHPLEQIKFLMGM--KGDAAVLIGGPWSPSLDGPNPERDPSVLVRTAIRCTKSMTGIDLSACTQWFRFAEVRYVHSGE-- 430
Cdd:pfam14443   1 VHPCKLLKFLVGDrgKDNEIMAIGGPWSPSLDGADPTTDPSVLIRTAIRTTKALTGIDLSNCTQWYRFAEVHYYRPKTdg 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 556966607  431 -SAQVETVVIFLPDVWQCVPSLLEWEAMSVQHNEAPSDSVMSA 472
Cdd:pfam14443  81 fPSRQEITVIFLPDVSSCLPSLEEWESLWLQYRKALLEKEREA 123
S1-like pfam14444
S1-like; S1-like RNA binding domain found in DBC1
 65-122 9.75e-32

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


:

Pssm-ID: 464176  Cd Length: 58  Bit Score: 117.86  E-value: 9.75e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 556966607   65 QRVITGVVTKLHDYFGVVDEDVIFQISAVNGRIPQVGEKVLVTAIYDPKVSMNWNAVK 122
Cdd:pfam14444   1 QRVFTGVVTKLQDYFGFVDEDVFFQLSVVKGRLPQVGDRVLVEAVYNPNMPFKWNAQR 58
BURAN pfam19257
BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.
 252-333 6.97e-28

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


:

Pssm-ID: 466013  Cd Length: 82  Bit Score: 107.40  E-value: 6.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607  252 SSYCDTMEVLRRYSNIPVPLDFFDARLCWVDSFPLSRPLSLEYPCHFHIVEREAETAEENIAELNPPDADhSYSAKVMLL 331
Cdd:pfam19257   2 SVERDYLELRKRYPRLYIPSDFSKLVLCWVETFPPLSPLPLDTPVSFHVMEKEVEPPLEQPAEAALEPAD-RYNAKVMLL 80


                  ..
gi 556966607  332 SS 333
Cdd:pfam19257  81 SG 82
LAIKA pfam19256
LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.
 492-562 2.64e-21

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


:

Pssm-ID: 466012 [Multi-domain]  Cd Length: 68  Bit Score: 88.45  E-value: 2.64e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556966607  492 LPEQPAIIVHPNRKFMSGEFSCAVLTLNTLFNYRTQMWREamlHSFEALLVSELFHEMLQRDFGFRIFKAL 562
Cdd:pfam19256   1 LPAEPAILVRPNRLAKGGKFDCKSLSLDGLLDYREDDTKE---STFEVSLFAELFHEMLQRDFGFTIYKAL 68
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
817-936 2.25e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 817 KNSDFVLLNGGLVHVGTLLEKLERSESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKA 896
Cdd:COG4372   12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 556966607 897 AEKLKTDCQRRLKENSKGLMSLTEQIQKLVNRTNSLIEEK 936
Cdd:COG4372   92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
676-936 2.32e-03

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 676 GVSLEDEERKsnasNLSELESGSLQEIDKELKTIVLLPRDVLLSFVYFDHNLCG---YIRHKQLEELLYTLGLHLSKAQV 752
Cdd:PRK03918 442 GRELTEEHRK----ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseLIKLKELAEQLKELEEKLKKYNL 517

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 753 RPLVKKvitnhACYYRKLN--YSETEWAIDSLSSKIHIHEDLlqgNQKLLPTSSHSSTSEKQKTDIKNSdfvLLNGGLVH 830
Cdd:PRK03918 518 EELEKK-----AEEYEKLKekLIKLKGEIKSLKKELEKLEEL---KKKLAELEKKLDELEEELAELLKE---LEELGFES 586

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 831 VGTLLEKLERSES------------SRIQ-MEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLaeTEEKLKAA 897
Cdd:PRK03918 587 VEELEERLKELEPfyneylelkdaeKELErEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEEL 664

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 556966607 898 EKLKTDCQRRLKENSKGLMSLTEQIQKLVNRTNSLIEEK 936
Cdd:PRK03918 665 REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
 
Name Accession Description Interval E-value
DBC1 pfam14443
DBC1; DBC1 and it homologs from diverse eukaryotes are a catalytically inactive version of the ...
 355-472 7.22e-58

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: 194.10  E-value: 7.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607  355 QHPLEQIKFLMGM--KGDAAVLIGGPWSPSLDGPNPERDPSVLVRTAIRCTKSMTGIDLSACTQWFRFAEVRYVHSGE-- 430
Cdd:pfam14443   1 VHPCKLLKFLVGDrgKDNEIMAIGGPWSPSLDGADPTTDPSVLIRTAIRTTKALTGIDLSNCTQWYRFAEVHYYRPKTdg 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 556966607  431 -SAQVETVVIFLPDVWQCVPSLLEWEAMSVQHNEAPSDSVMSA 472
Cdd:pfam14443  81 fPSRQEITVIFLPDVSSCLPSLEEWESLWLQYRKALLEKEREA 123
S1-like pfam14444
S1-like; S1-like RNA binding domain found in DBC1
 65-122 9.75e-32

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


Pssm-ID: 464176  Cd Length: 58  Bit Score: 117.86  E-value: 9.75e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 556966607   65 QRVITGVVTKLHDYFGVVDEDVIFQISAVNGRIPQVGEKVLVTAIYDPKVSMNWNAVK 122
Cdd:pfam14444   1 QRVFTGVVTKLQDYFGFVDEDVFFQLSVVKGRLPQVGDRVLVEAVYNPNMPFKWNAQR 58
BURAN pfam19257
BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.
 252-333 6.97e-28

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


Pssm-ID: 466013  Cd Length: 82  Bit Score: 107.40  E-value: 6.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607  252 SSYCDTMEVLRRYSNIPVPLDFFDARLCWVDSFPLSRPLSLEYPCHFHIVEREAETAEENIAELNPPDADhSYSAKVMLL 331
Cdd:pfam19257   2 SVERDYLELRKRYPRLYIPSDFSKLVLCWVETFPPLSPLPLDTPVSFHVMEKEVEPPLEQPAEAALEPAD-RYNAKVMLL 80


                  ..
gi 556966607  332 SS 333
Cdd:pfam19257  81 SG 82
LAIKA pfam19256
LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.
 492-562 2.64e-21

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


Pssm-ID: 466012 [Multi-domain]  Cd Length: 68  Bit Score: 88.45  E-value: 2.64e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556966607  492 LPEQPAIIVHPNRKFMSGEFSCAVLTLNTLFNYRTQMWREamlHSFEALLVSELFHEMLQRDFGFRIFKAL 562
Cdd:pfam19256   1 LPAEPAILVRPNRLAKGGKFDCKSLSLDGLLDYREDDTKE---STFEVSLFAELFHEMLQRDFGFTIYKAL 68
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
817-936 2.25e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 817 KNSDFVLLNGGLVHVGTLLEKLERSESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKA 896
Cdd:COG4372   12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 556966607 897 AEKLKTDCQRRLKENSKGLMSLTEQIQKLVNRTNSLIEEK 936
Cdd:COG4372   92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 833-939 1.11e-05

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 49.08  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607  833 TLLEKLERSESSRIQMEKKIDSLKTQLGEATAQ----VAEVDAVNKS-------------LTTELQELQKRLAETEEKLK 895
Cdd:pfam06160 274 QLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQnkelKEELERVQQSytlnenelervrgLEKQLEELEKRYDEIVERLE 353

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 556966607  896 AAEKLKTDCQRRLKENSKGLMSLTEQIQKLVNRTNSLIEEKMDA 939
Cdd:pfam06160 354 EKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEA 397
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 834-936 2.70e-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: 48.13  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607   834 LLEKLERSESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLKENSK 913
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316

                           90       100
                   ....*....|....*....|...
gi 556966607   914 GLMSLTEQIQKLVNRTNSLIEEK 936
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEEL 339
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
676-936 2.32e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 676 GVSLEDEERKsnasNLSELESGSLQEIDKELKTIVLLPRDVLLSFVYFDHNLCG---YIRHKQLEELLYTLGLHLSKAQV 752
Cdd:PRK03918 442 GRELTEEHRK----ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseLIKLKELAEQLKELEEKLKKYNL 517

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 753 RPLVKKvitnhACYYRKLN--YSETEWAIDSLSSKIHIHEDLlqgNQKLLPTSSHSSTSEKQKTDIKNSdfvLLNGGLVH 830
Cdd:PRK03918 518 EELEKK-----AEEYEKLKekLIKLKGEIKSLKKELEKLEEL---KKKLAELEKKLDELEEELAELLKE---LEELGFES 586

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 831 VGTLLEKLERSES------------SRIQ-MEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLaeTEEKLKAA 897
Cdd:PRK03918 587 VEELEERLKELEPfyneylelkdaeKELErEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEEL 664

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 556966607 898 EKLKTDCQRRLKENSKGLMSLTEQIQKLVNRTNSLIEEK 936
Cdd:PRK03918 665 REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 833-939 3.43e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.97  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 833 TLLEKLERSESSRIQMEKKIDSLKTQLGEATAQ----VAEVDAVNKS-------------LTTELQELQKRLAETEEKLK 895
Cdd:PRK04778 293 QLYDILEREVKARKYVEKNSDTLPDFLEHAKEQnkelKEEIDRVKQSytlneselesvrqLEKQLESLEKQYDEITERIA 372

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 556966607 896 AAEKLKTDCQRRLKENSKGLMSLTEQIQKLVNRTNSLIEEKMDA 939
Cdd:PRK04778 373 EQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEA 416
 
Name Accession Description Interval E-value
DBC1 pfam14443
DBC1; DBC1 and it homologs from diverse eukaryotes are a catalytically inactive version of the ...
 355-472 7.22e-58

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: 194.10  E-value: 7.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607  355 QHPLEQIKFLMGM--KGDAAVLIGGPWSPSLDGPNPERDPSVLVRTAIRCTKSMTGIDLSACTQWFRFAEVRYVHSGE-- 430
Cdd:pfam14443   1 VHPCKLLKFLVGDrgKDNEIMAIGGPWSPSLDGADPTTDPSVLIRTAIRTTKALTGIDLSNCTQWYRFAEVHYYRPKTdg 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 556966607  431 -SAQVETVVIFLPDVWQCVPSLLEWEAMSVQHNEAPSDSVMSA 472
Cdd:pfam14443  81 fPSRQEITVIFLPDVSSCLPSLEEWESLWLQYRKALLEKEREA 123
S1-like pfam14444
S1-like; S1-like RNA binding domain found in DBC1
 65-122 9.75e-32

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


Pssm-ID: 464176  Cd Length: 58  Bit Score: 117.86  E-value: 9.75e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 556966607   65 QRVITGVVTKLHDYFGVVDEDVIFQISAVNGRIPQVGEKVLVTAIYDPKVSMNWNAVK 122
Cdd:pfam14444   1 QRVFTGVVTKLQDYFGFVDEDVFFQLSVVKGRLPQVGDRVLVEAVYNPNMPFKWNAQR 58
BURAN pfam19257
BURAN domain; This presumed domain is found exclusively in the CCAR1 protein.
 252-333 6.97e-28

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


Pssm-ID: 466013  Cd Length: 82  Bit Score: 107.40  E-value: 6.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607  252 SSYCDTMEVLRRYSNIPVPLDFFDARLCWVDSFPLSRPLSLEYPCHFHIVEREAETAEENIAELNPPDADhSYSAKVMLL 331
Cdd:pfam19257   2 SVERDYLELRKRYPRLYIPSDFSKLVLCWVETFPPLSPLPLDTPVSFHVMEKEVEPPLEQPAEAALEPAD-RYNAKVMLL 80


                  ..
gi 556966607  332 SS 333
Cdd:pfam19257  81 SG 82
LAIKA pfam19256
LAIKA domain; This presumed domain is found exclusively in the CCAR1 protein.
 492-562 2.64e-21

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


Pssm-ID: 466012 [Multi-domain]  Cd Length: 68  Bit Score: 88.45  E-value: 2.64e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556966607  492 LPEQPAIIVHPNRKFMSGEFSCAVLTLNTLFNYRTQMWREamlHSFEALLVSELFHEMLQRDFGFRIFKAL 562
Cdd:pfam19256   1 LPAEPAILVRPNRLAKGGKFDCKSLSLDGLLDYREDDTKE---STFEVSLFAELFHEMLQRDFGFTIYKAL 68
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
817-936 2.25e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 817 KNSDFVLLNGGLVHVGTLLEKLERSESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKA 896
Cdd:COG4372   12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 556966607 897 AEKLKTDCQRRLKENSKGLMSLTEQIQKLVNRTNSLIEEK 936
Cdd:COG4372   92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 833-939 1.11e-05

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 49.08  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607  833 TLLEKLERSESSRIQMEKKIDSLKTQLGEATAQ----VAEVDAVNKS-------------LTTELQELQKRLAETEEKLK 895
Cdd:pfam06160 274 QLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQnkelKEELERVQQSytlnenelervrgLEKQLEELEKRYDEIVERLE 353

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 556966607  896 AAEKLKTDCQRRLKENSKGLMSLTEQIQKLVNRTNSLIEEKMDA 939
Cdd:pfam06160 354 EKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEA 397
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 834-936 2.70e-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: 48.13  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607   834 LLEKLERSESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLKENSK 913
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316

                           90       100
                   ....*....|....*....|...
gi 556966607   914 GLMSLTEQIQKLVNRTNSLIEEK 936
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEEL 339
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 847-937 5.09e-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: 45.69  E-value: 5.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 847 QMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLKE---------NSKGLMS 917
Cdd:COG1579   14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlgnvrNNKEYEA 93

                         90       100
                 ....*....|....*....|
gi 556966607 918 LTEQIQKLvNRTNSLIEEKM 937
Cdd:COG1579   94 LQKEIESL-KRRISDLEDEI 112
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 836-932 1.92e-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: 44.75  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 836 EKLERSESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLKENSKGL 915
Cdd:COG4942  129 EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208

                         90
                 ....*....|....*..
gi 556966607 916 MSLTEQIQKLVNRTNSL 932
Cdd:COG4942  209 AELAAELAELQQEAEEL 225
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 836-926 2.24e-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: 44.75  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 836 EKLERSESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLKENSKGL 915
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90
                 ....*....|.
gi 556966607 916 MSLTEQIQKLV 926
Cdd:COG4942  100 EAQKEELAELL 110
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 841-925 2.69e-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: 44.37  E-value: 2.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 841 SESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLKENSKGLMSLTE 920
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97


                 ....*
gi 556966607 921 QIQKL 925
Cdd:COG4942   98 ELEAQ 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 834-939 5.16e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 5.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 834 LLEKLERSESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQ-------KRLAETEEKLKAAEKLKTDCQR 906
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQaeeyellAELARLEQDIARLEERRRELEE 316

                         90       100       110
                 ....*....|....*....|....*....|...
gi 556966607 907 RLKENSKGLMSLTEQIQKLVNRTNSLIEEKMDA 939
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEA 349
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
836-925 7.09e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 42.12  E-value: 7.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 836 EKLERSESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKAA-----EKLKTDCQRRLKE 910
Cdd:COG1842   16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLAlekgrEDLAREALERKAE 95

                         90
                 ....*....|....*
gi 556966607 911 NSKGLMSLTEQIQKL 925
Cdd:COG1842   96 LEAQAEALEAQLAQL 110
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 841-910 7.21e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 7.21e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 841 SESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLKE 910
Cdd:COG3883   14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 831-935 8.35e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.22  E-value: 8.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 831 VGTLLEKLERSESSRIQMEKKIDSLKTQLGEATAQVaEVDAVNK---SLTTELQELQKRLAETEEKLKAAEKLKTDCQRR 907
Cdd:COG1579   54 LEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKeieSLKRRISDLEDEILELMERIEELEEELAELEAE 132

                         90       100
                 ....*....|....*....|....*...
gi 556966607 908 LKENSKGLMSLTEQIQKLVNRTNSLIEE 935
Cdd:COG1579  133 LAELEAELEEKKAELDEELAELEAELEE 160
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
836-935 8.37e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 8.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 836 EKLERSESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLKENSKGL 915
Cdd:COG4372   66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145

                         90       100
                 ....*....|....*....|
gi 556966607 916 MSLTEQIQKLVNRTNSLIEE 935
Cdd:COG4372  146 AEREEELKELEEQLESLQEE 165
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
836-936 9.53e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 9.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 836 EKLERSESSRIQMEKKIDSLKTQLGEATAQVAEvdavnksLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLKENSKGL 915
Cdd:COG4372   87 EQLQAAQAELAQAQEELESLQEEAEELQEELEE-------LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159

                         90       100
                 ....*....|....*....|.
gi 556966607 916 MSLTEQIQKLVNRTNSLIEEK 936
Cdd:COG4372  160 ESLQEELAALEQELQALSEAE 180
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 836-901 1.29e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.29e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556966607 836 EKLERSESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKAA-EKLK 901
Cdd:COG3883   23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERrEELG 89
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
834-925 1.37e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607  834 LLEKLERSESSRIqmekKIDSLKTQLGEATAQVAEVDAVNKslttELQELQKRLAETEEKLKAAEKLKTDCQRRLKENSK 913
Cdd:COG4913   649 ALQRLAEYSWDEI----DVASAEREIAELEAELERLDASSD----DLAALEEQLEELEAELEELEEELDELKGEIGRLEK 720

                          90
                  ....*....|..
gi 556966607  914 GLMSLTEQIQKL 925
Cdd:COG4913   721 ELEQAEEELDEL 732
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 837-910 1.57e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 1.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556966607 837 KLERSESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLKE 910
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
833-925 1.88e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 833 TLLEKLERSESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLKENS 912
Cdd:COG4372   42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121

                         90
                 ....*....|...
gi 556966607 913 KGLMSLTEQIQKL 925
Cdd:COG4372  122 KERQDLEQQRKQL 134
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 830-934 1.97e-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: 41.97  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607   830 HVGTLLEKLERSESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLK 909
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                           90       100
                   ....*....|....*....|....*
gi 556966607   910 ENSKGLMSLTEQIQKLVNRTNSLIE 934
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDNLQE 943
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 849-932 2.29e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 849 EKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLKENSKglmSLTEQIQKLVNR 928
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---EIEERREELGER 91


                 ....
gi 556966607 929 TNSL 932
Cdd:COG3883   92 ARAL 95
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
676-936 2.32e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 676 GVSLEDEERKsnasNLSELESGSLQEIDKELKTIVLLPRDVLLSFVYFDHNLCG---YIRHKQLEELLYTLGLHLSKAQV 752
Cdd:PRK03918 442 GRELTEEHRK----ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseLIKLKELAEQLKELEEKLKKYNL 517

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 753 RPLVKKvitnhACYYRKLN--YSETEWAIDSLSSKIHIHEDLlqgNQKLLPTSSHSSTSEKQKTDIKNSdfvLLNGGLVH 830
Cdd:PRK03918 518 EELEKK-----AEEYEKLKekLIKLKGEIKSLKKELEKLEEL---KKKLAELEKKLDELEEELAELLKE---LEELGFES 586

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 831 VGTLLEKLERSES------------SRIQ-MEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLaeTEEKLKAA 897
Cdd:PRK03918 587 VEELEERLKELEPfyneylelkdaeKELErEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEEL 664

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 556966607 898 EKLKTDCQRRLKENSKGLMSLTEQIQKLVNRTNSLIEEK 936
Cdd:PRK03918 665 REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 833-907 2.62e-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: 39.22  E-value: 2.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556966607  833 TLLEKLERSESSRIQMEKKIDSLKTQLGEATAQVAevdavnkSLTTELQELQKRLAETEEKLKA----AEKLKTDCQRR 907
Cdd:pfam11559  56 SLNETIRTLEAEIERLQSKIERLKTQLEDLERELA-------LLQAKERQLEKKLKTLEQKLKNekeeLQRLKNALQQI 127
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
849-936 2.72e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607  849 EKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKR----------------LAETEEKLKAAEKLKtdcqRRLKENS 912
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAELEAEL----ERLDASS 684

                          90       100
                  ....*....|....*....|....
gi 556966607  913 KGLMSLTEQIQKLVNRTNSLIEEK 936
Cdd:COG4913   685 DDLAALEEQLEELEAELEELEEEL 708
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
831-935 3.02e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 831 VGTLLEKLERSESSRIQMEKKIDSLKTQLGEATAQVAEV--DAVNKSLTTELQELQKRLAE-----TEE--KLKAAEKLK 901
Cdd:COG3206  221 LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAElsaryTPNhpDVIALRAQI 300

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 556966607 902 TDCQRRLKENSKGLMSLTE-QIQKLVNRTNSLIEE 935
Cdd:COG3206  301 AALRAQLQQEAQRILASLEaELEALQAREASLQAQ 335
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 833-939 3.43e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.97  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 833 TLLEKLERSESSRIQMEKKIDSLKTQLGEATAQ----VAEVDAVNKS-------------LTTELQELQKRLAETEEKLK 895
Cdd:PRK04778 293 QLYDILEREVKARKYVEKNSDTLPDFLEHAKEQnkelKEEIDRVKQSytlneselesvrqLEKQLESLEKQYDEITERIA 372

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 556966607 896 AAEKLKTDCQRRLKENSKGLMSLTEQIQKLVNRTNSLIEEKMDA 939
Cdd:PRK04778 373 EQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEA 416
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 833-935 4.05e-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: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607   833 TLLEKLERSESSRIQMEKKIDSLKTQLGEATAQVAEVDAVNKSLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLKENS 912
Cdd:TIGR02168  702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781

                           90       100
                   ....*....|....*....|...
gi 556966607   913 KGLMSLTEQIQKLVNRTNSLIEE 935
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREA 804
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 850-925 4.16e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 39.50  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607  850 KKIDSLKTQLGEATAQ-------VAEVDAVNKSLTTELQELQKRLAETEEKLKAAEKLKTdcqrRLKENSKGLMSLTEQI 922
Cdd:pfam13851  26 ELIKSLKEEIAELKKKeerneklMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQ----SLKNLKARLKVLEKEL 101


                  ...
gi 556966607  923 QKL 925
Cdd:pfam13851 102 KDL 104
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 779-937 4.75e-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: 40.93  E-value: 4.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607   779 IDSLSSKIHIHEDLLQ--GNQKLlptssHSSTSEKQKTDIKNSdfvllngglvhvgtLLEKLERSESSRIQMEKKIDSLK 856
Cdd:pfam01576  463 VSSLESQLQDTQELLQeeTRQKL-----NLSTRLRQLEDERNS--------------LQEQLEEEEEAKRNVERQLSTLQ 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607   857 TQLGEATAQVAEVDAV-------NKSLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLKE------NSKGLMSLTEQIQ 923
Cdd:pfam01576  524 AQLSDMKKKLEEDAGTlealeegKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDllvdldHQRQLVSNLEKKQ 603

                          170
                   ....*....|....
gi 556966607   924 KLVNRTnsLIEEKM 937
Cdd:pfam01576  604 KKFDQM--LAEEKA 615
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 833-935 4.93e-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: 40.81  E-value: 4.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607   833 TLLEKLERSESSRIQMEKKIDSLKTQLGEATAQVAEvdavnksLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLKENS 912
Cdd:TIGR02168  264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISR-------LEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336

                           90       100
                   ....*....|....*....|...
gi 556966607   913 KGLMSLTEQIQKLVNRTNSLIEE 935
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLEAE 359
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 834-935 6.37e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 6.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607 834 LLEKLERSESSRIQMEKKIDSLKTQLGEATAQVAEvdavnksLTTELQELQKRLAETEEKLKAAEKLKTDCQRRLKENSK 913
Cdd:COG1196  286 AQAEEYELLAELARLEQDIARLEERRRELEERLEE-------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358

                         90       100
                 ....*....|....*....|..
gi 556966607 914 GLMSLTEQIQKLVNRTNSLIEE 935
Cdd:COG1196  359 ELAEAEEALLEAEAELAEAEEE 380
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 832-939 8.60e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 38.40  E-value: 8.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556966607  832 GTLLEKLE-RSESSRIQMEKKIDSLKTQLGEATAQVAE-----VDAVNKSLTTELQELQKRLAETEEKLKA-----AEKL 900
Cdd:pfam01442  47 EEVRAKLEpYLEELQAKLGQNVEELRQRLEPYTEELRKrlnadAEELQEKLAPYGEELRERLEQNVDALRArlapyAEEL 126

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 556966607  901 KTDCQRRLKENSKGLMSLTEQIQKLVNRTNSLIEEKMDA 939
Cdd:pfam01442 127 RQKLAERLEELKESLAPYAEEVQAQLSQRLQELREKLEP 165
 
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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