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Conserved domains on  [gi|1907183035|ref|XP_036009188|]
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transforming acidic coiled-coil-containing protein 2 isoform X32 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 837-1040 2.82e-98

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


:

Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 308.53  E-value: 2.82e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  837 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIgkpEDEQREKSISHQTVQQLVLEK 916
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMI---EEKQKQKELEHAEIQKVLEEK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  917 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGK 996
Cdd:pfam05010   78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907183035  997 AQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 1040
Cdd:pfam05010  158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
PRK13335 super family cl31400
superantigen-like protein SSL3; Reviewed;
202-313 1.88e-04

superantigen-like protein SSL3; Reviewed;


The actual alignment was detected with superfamily member PRK13335:

Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 45.12  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  202 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 274
Cdd:PRK13335    45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1907183035  275 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 313
Cdd:PRK13335   125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
540-793 6.98e-03

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK08691:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 709  Bit Score: 40.46  E-value: 6.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  540 PPSQD-PTPAATPEAPSAIST-VVHATDEEKLAVTSQKWTCMTVDLDADKQDFPQPSDlsNFVNETKFNSPSEELDYrnS 617
Cdd:PRK08691   434 PPWEDaPDEAQTAAGTAQTSAkSIQTASEAETPPENQVSKNKAADNETDAPLSEVPSE--NPIQATPNDEAVETETF--A 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  618 YEIEYMEKLGSSLPQDDDTPKKQALYLMFDTPQESPVKSP---------PVRMSDSPTPCSGSSFEDTEalvNAATKLQH 688
Cdd:PRK08691   510 HEAPAEPFYGYGFPDNDCPPEDGAEIPPPDWEHAAPADTAgggadeeaeAGGIGGNNTPSAPPPEFSTE---NWAAIVRH 586

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  689 pVARGLPSSQEPLLQVPEKPSQKELEAMALGTPAEAIEITAPEGAFASADTLLSRLAHPASLcgALGYLEPDLAEKNPPV 768
Cdd:PRK08691   587 -FARKLGAAQMPAQHSAWTEYHPDTGLMVLAMTAEARATADKKRLDKIRDTLAQAYGLQLTL--QTQDWRDEAGRETPAM 663

                          250       260
                   ....*....|....*....|....*.
gi 1907183035  769 FAQKLQ-EELEFAVMRIEALKLARQI 793
Cdd:PRK08691   664 QDKRVQaEDRQKAQALLEADPAAQKI 689
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 837-1040 2.82e-98

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 308.53  E-value: 2.82e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  837 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIgkpEDEQREKSISHQTVQQLVLEK 916
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMI---EEKQKQKELEHAEIQKVLEEK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  917 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGK 996
Cdd:pfam05010   78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907183035  997 AQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 1040
Cdd:pfam05010  158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 770-1042 2.55e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 2.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  770 AQKLQEELEfaVMRIEALKLARQIALASRSRQDTKREAahppdvsisktalysrigstevekppgllfqqpdLDSALQVA 849
Cdd:COG1196    215 YRELKEELK--ELEAELLLLKLRELEAELEELEAELEE----------------------------------LEAELEEL 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  850 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEKS 929
Cdd:COG1196    259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  930 LADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLR 1009
Cdd:COG1196    339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907183035 1010 KEQLRVDALERTLEQKNKEIEELTKICDELIAK 1042
Cdd:COG1196    419 LEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
835-1034 1.70e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 1.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  835 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKT---IAQMigKPEDEQREKSIshQTVQQ 911
Cdd:PRK03918   184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEEL--EKELESLEGSK--RKLEE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  912 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA--- 988
Cdd:PRK03918   260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkee 338

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  989 --------------EIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTK 1034
Cdd:PRK03918   339 rleelkkklkelekRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 841-1042 1.02e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  841 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREksishqtVQQLVLEKEQAL 920
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE-------LTELEAEIEELE 767

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  921 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 1000
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907183035 1001 QAAYQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 1042
Cdd:TIGR02168  841 EDLEE---QIEELSED-----IESLAAEIEELEELIEELESE 874
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
202-313 1.88e-04

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 45.12  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  202 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 274
Cdd:PRK13335    45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1907183035  275 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 313
Cdd:PRK13335   125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
 540-793 6.98e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 40.46  E-value: 6.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  540 PPSQD-PTPAATPEAPSAIST-VVHATDEEKLAVTSQKWTCMTVDLDADKQDFPQPSDlsNFVNETKFNSPSEELDYrnS 617
Cdd:PRK08691   434 PPWEDaPDEAQTAAGTAQTSAkSIQTASEAETPPENQVSKNKAADNETDAPLSEVPSE--NPIQATPNDEAVETETF--A 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  618 YEIEYMEKLGSSLPQDDDTPKKQALYLMFDTPQESPVKSP---------PVRMSDSPTPCSGSSFEDTEalvNAATKLQH 688
Cdd:PRK08691   510 HEAPAEPFYGYGFPDNDCPPEDGAEIPPPDWEHAAPADTAgggadeeaeAGGIGGNNTPSAPPPEFSTE---NWAAIVRH 586

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  689 pVARGLPSSQEPLLQVPEKPSQKELEAMALGTPAEAIEITAPEGAFASADTLLSRLAHPASLcgALGYLEPDLAEKNPPV 768
Cdd:PRK08691   587 -FARKLGAAQMPAQHSAWTEYHPDTGLMVLAMTAEARATADKKRLDKIRDTLAQAYGLQLTL--QTQDWRDEAGRETPAM 663

                          250       260
                   ....*....|....*....|....*.
gi 1907183035  769 FAQKLQ-EELEFAVMRIEALKLARQI 793
Cdd:PRK08691   664 QDKRVQaEDRQKAQALLEADPAAQKI 689
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 837-1040 2.82e-98

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 308.53  E-value: 2.82e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  837 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIgkpEDEQREKSISHQTVQQLVLEK 916
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMI---EEKQKQKELEHAEIQKVLEEK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  917 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGK 996
Cdd:pfam05010   78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907183035  997 AQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 1040
Cdd:pfam05010  158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 770-1042 2.55e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 2.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  770 AQKLQEELEfaVMRIEALKLARQIALASRSRQDTKREAahppdvsisktalysrigstevekppgllfqqpdLDSALQVA 849
Cdd:COG1196    215 YRELKEELK--ELEAELLLLKLRELEAELEELEAELEE----------------------------------LEAELEEL 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  850 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEKS 929
Cdd:COG1196    259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  930 LADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLR 1009
Cdd:COG1196    339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907183035 1010 KEQLRVDALERTLEQKNKEIEELTKICDELIAK 1042
Cdd:COG1196    419 LEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
835-1034 1.70e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 1.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  835 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKT---IAQMigKPEDEQREKSIshQTVQQ 911
Cdd:PRK03918   184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEEL--EKELESLEGSK--RKLEE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  912 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA--- 988
Cdd:PRK03918   260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkee 338

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  989 --------------EIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTK 1034
Cdd:PRK03918   339 rleelkkklkelekRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
896-1043 6.66e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 6.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  896 EDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADL---FRRYEKMKEVLEGFRKNEEvLKKCAQEYLSRVKKEEQRY 972
Cdd:COG4717     77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeLEKLEKLLQLLPLYQELEA-LEAELAELPERLEELEERL 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  973 QALKvHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKE-----------QLRVDALERTLEQKNKEIEELTKICDELIA 1041
Cdd:COG4717    156 EELR-ELEEELEELEAELAELQEELEELLEQLSLATEEElqdlaeeleelQQRLAELEEELEEAQEELEELEEELEQLEN 234


                   ..
gi 1907183035 1042 KM 1043
Cdd:COG4717    235 EL 236
PTZ00121 PTZ00121
MAEBL; Provisional
 781-1034 8.95e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 8.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  781 VMRIEALKLARQIALASRSRQDTKREAAHPPDVSISKTALYSRIGSTEVEKPPGLLFQQPDLDSALQV-ARAEVIAKERE 859
Cdd:PTZ00121  1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEE 1630

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  860 ----VSEWRDKYEESRREVVEMRKiVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFR 935
Cdd:PTZ00121  1631 ekkkVEQLKKKEAEEKKKAEELKK-AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  936 RYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKldranAEIAQVrgKAQQEQAAYQASLRKEQLRV 1015
Cdd:PTZ00121  1710 KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK-----KKIAHL--KKEEEKKAEEIRKEKEAVIE 1782

                          250
                   ....*....|....*....
gi 1907183035 1016 DALERTLEQKNKEIEELTK 1034
Cdd:PTZ00121  1783 EELDEEDEKRRMEVDKKIK 1801
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 841-1042 1.02e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  841 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREksishqtVQQLVLEKEQAL 920
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE-------LTELEAEIEELE 767

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  921 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 1000
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907183035 1001 QAAYQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 1042
Cdd:TIGR02168  841 EDLEE---QIEELSED-----IESLAAEIEELEELIEELESE 874
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 838-1042 1.45e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.61  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  838 QQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIaqmigkpedEQREKSISHQTVQQLVLEKE 917
Cdd:COG4942     49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---------EAQKEELAELLRALYRLGRQ 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  918 QALADLNSVEkSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKA 997
Cdd:COG4942    120 PPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907183035  998 QQEqaayqasLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 1042
Cdd:COG4942    198 QKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAE 235
PTZ00121 PTZ00121
MAEBL; Provisional
 845-1042 1.52e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 1.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  845 ALQVARAEVIAKErevSEWRDKYEESRREVVEMRKivAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALAD-- 922
Cdd:PTZ00121  1453 AEEAKKAEEAKKK---AEEAKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADea 1527

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  923 LNSVEKSLADLFRRYEKMKEVLEgFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQA 1002
Cdd:PTZ00121  1528 KKAEEAKKADEAKKAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907183035 1003 AYQASLRK-EQLRVDALE-RTLEQKNKEIEELTKICDELIAK 1042
Cdd:PTZ00121  1607 MKAEEAKKaEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKK 1648
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 832-1034 3.10e-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: 3.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  832 PPGLLFQQPDLDSALQVARAEVIAK-EREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQ 910
Cdd:TIGR02168  657 PGGVITGGSAKTNSSILERRREIEElEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  911 QLVLEKEQALADLNSVEKSLADLfrrYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANAEI 990
Cdd:TIGR02168  737 RLEAEVEQLEERIAQLSKELTEL---EAEIEELEERLEEAEEELAEAEAE-IEELEAQIEQLKEELKALREALDELRAEL 812

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907183035  991 AQVRGKAQQEQAAYQASLRK---EQLRVDALERTLEQKNKEIEELTK 1034
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRiaaTERRLEDLEEQIEELSEDIESLAA 859
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 848-1041 3.20e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 3.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  848 VARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIA---QMIGKPEDEqREKSISHQTVQQ---------LVLE 915
Cdd:TIGR02169  153 VERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDekrQQLERLRRE-REKAERYQALLKekreyegyeLLKE 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  916 KEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKE-EQRYQALKvhaeEKLDRANAEIAQVR 994
Cdd:TIGR02169  232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVK----EKIGELEAEIASLE 307

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907183035  995 GKAQQEQAAYQAS---LRKEQLRVDALERTLEQKNKEIEELTKICDELIA 1041
Cdd:TIGR02169  308 RSIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 838-1025 3.58e-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: 3.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  838 QQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREksisHQTVQQLVLEKE 917
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ----LETLRSKVAQLE 392

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  918 QALADLNS----VEKSLADLFRRYEKMKEVLEGFRKN-EEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQ 992
Cdd:TIGR02168  393 LQIASLNNeierLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1907183035  993 VRgkaqQEQAAYQASLRKEQLRVDALERTLEQK 1025
Cdd:TIGR02168  473 AE----QALDAAERELAQLQARLDSLERLQENL 501
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 873-1032 3.87e-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: 47.74  E-value: 3.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  873 EVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVL---EKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRK 949
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLevsELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  950 NEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEI 1029
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-----------LEELEAELEELESRLEELEEQL 381


                   ...
gi 1907183035 1030 EEL 1032
Cdd:TIGR02168  382 ETL 384
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
831-1034 8.07e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 8.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  831 KPPGLLFQQPDLDSALQVARAEV---IAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAqmigkpedeqreksishq 907
Cdd:COG4717     65 KPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQ------------------ 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  908 tVQQLVLEKEQAladlnsvEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRAN 987
Cdd:COG4717    127 -LLPLYQELEAL-------EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907183035  988 AEIAQVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEIEELTK 1034
Cdd:COG4717    199 EELEELQQR-----------LAELEEELEEAQEELEELEEELEQLEN 234
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 771-1042 1.33e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  771 QKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAhppdvsisKTALYsrigstevekppgllfqqpDLDSALQVAR 850
Cdd:COG1196    235 RELEAELEELEAELEELEAELEELEAELAELEAELEEL--------RLELE-------------------ELELELEEAQ 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  851 AEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSL 930
Cdd:COG1196    288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  931 ADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRG--KAQQEQAAYQASL 1008
Cdd:COG1196    368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEleEEEEEEEEALEEA 447

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1907183035 1009 RKEQLRVDALERTLEQKNKEIEELTKICDELIAK 1042
Cdd:COG1196    448 AEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
202-313 1.88e-04

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 45.12  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  202 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 274
Cdd:PRK13335    45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1907183035  275 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 313
Cdd:PRK13335   125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 771-1040 7.55e-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: 43.52  E-value: 7.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  771 QKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAhppdvsISKTALYSRIGSTEVEKppgLLFQQPDLDSALQVAR 850
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA------ERYQALLKEKREYEGYE---LLKEKEALERQKEAIE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  851 AEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMigkPEDEQRE--KSISHQTVQQLVLEKEQALADLN--SV 926
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL---GEEEQLRvkEKIGELEAEIASLERSIAEKEREleDA 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  927 EKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEkLDRANAEiaqvrgkaqqeqaayqa 1006
Cdd:TIGR02169  321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE-VDKEFAE----------------- 382

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1907183035 1007 sLRKEQlrvDALERTLEQKNKEIEELTKICDELI 1040
Cdd:TIGR02169  383 -TRDEL---KDYREKLEKLKREINELKRELDRLQ 412
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
857-1045 1.37e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  857 EREVSEWRDKYEESRREVVEMRKIVAEYE--KTIAQMIGKPEDEQREKSIshqtvqqlvleKEQALADLNSVEKSLADLF 934
Cdd:PRK03918   404 EEEISKITARIGELKKEIKELKKAIEELKkaKGKCPVCGRELTEEHRKEL-----------LEEYTAELKRIEKELKEIE 472

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  935 RRYEKMKEV---LEGFRKNEEVLKKcAQEYLSRVKKEEQRyqaLKVHAEEKLDRANAEIAQVRGKAQQEQAAYQaSLRKE 1011
Cdd:PRK03918   473 EKERKLRKElreLEKVLKKESELIK-LKELAEQLKELEEK---LKKYNLEELEKKAEEYEKLKEKLIKLKGEIK-SLKKE 547

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1907183035 1012 QLRVDALERTLEQKNKEIEELTKICDELIAKMGK 1045
Cdd:PRK03918   548 LEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
PTZ00121 PTZ00121
MAEBL; Provisional
 841-1042 1.39e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  841 DLDSALQVARAEVIAKEREV--SEWRDKYEESRREvvEMRKIVAEYEKTIAQMIgkpeDEQREKSISHQTVQQLVLEKEQ 918
Cdd:PTZ00121  1538 EAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKA--EEDKNMALRKAEEAKKA----EEARIEEVMKLYEEEKKMKAEE 1611

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  919 AladlnsveksladlfRRYEKMKEVLEGFRKNEEVLKKCAQeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQvrgKAQ 998
Cdd:PTZ00121  1612 A---------------KKAEEAKIKAEELKKAEEEKKKVEQ---LKKKEAEEKKKAEELKKAEEENKIKAAEEA---KKA 1670

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907183035  999 QEQAAYQASLRKEQ----LRVDALERTLEQKNKeIEELTKICDELIAK 1042
Cdd:PTZ00121  1671 EEDKKKAEEAKKAEedekKAAEALKKEAEEAKK-AEELKKKEAEEKKK 1717
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
853-1041 1.55e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  853 VIAKEREVSEWRDKYE-----ESRREVVEMRKIVA---EYEKTIAQMIG-KPEDEQREKSISHqtVQQLVLEKEQALADL 923
Cdd:PRK03918   488 VLKKESELIKLKELAEqlkelEEKLKKYNLEELEKkaeEYEKLKEKLIKlKGEIKSLKKELEK--LEELKKKLAELEKKL 565

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  924 NSVEKSLADLFRRYEKmkevlEGFRKNEEV------LKKCAQEYL------SRVKKEEQRYQALK---VHAEEKLDRANA 988
Cdd:PRK03918   566 DELEEELAELLKELEE-----LGFESVEELeerlkeLEPFYNEYLelkdaeKELEREEKELKKLEeelDKAFEELAETEK 640

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907183035  989 EIAQVRGK----AQQEQAAYQASLRKEQLRvdaLERTLEQKNKEIEELTKICDELIA 1041
Cdd:PRK03918   641 RLEELRKEleelEKKYSEEEYEELREEYLE---LSRELAGLRAELEELEKRREEIKK 694
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 770-1028 2.13e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  770 AQKLQEELEfavmriealKLARQIALASRSRQDTKREAAhppdvsisktalysrigstevekppGLLFQQPDLDSALQVA 849
Cdd:COG4942     22 AAEAEAELE---------QLQQEIAELEKELAALKKEEK-------------------------ALLKQLAALERRIAAL 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  850 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEKS 929
Cdd:COG4942     68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  930 LADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRgKAQQEQAAYQASLR 1009
Cdd:COG4942    148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELE 226

                          250
                   ....*....|....*....
gi 1907183035 1010 KEqlrVDALERTLEQKNKE 1028
Cdd:COG4942    227 AL---IARLEAEAAAAAER 242
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
841-1045 2.48e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  841 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQAL 920
Cdd:COG4372     63 QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  921 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKcaQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 1000
Cdd:COG4372    143 SEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEEL 220

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907183035 1001 QAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGK 1045
Cdd:COG4372    221 LEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
909-1033 5.39e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 5.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  909 VQQLVLEKEQALADLNsvekSLADLFRRYEKMKEVLEGFRKNEEVL---KKCAQEYLS-RVKKEEQRYQALKVH---AEE 981
Cdd:COG4913    213 VREYMLEEPDTFEAAD----ALVEHFDDLERAHEALEDAREQIELLepiRELAERYAAaRERLAELEYLRAALRlwfAQR 288

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907183035  982 KLDRANAEIAQVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEIEELT 1033
Cdd:COG4913    289 RLELLEAELEELRAE-----------LARLEAELERLEARLDALREELDELE 329
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
841-1042 5.96e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 5.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  841 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQR-EKSISH-----QTvQQLVL 914
Cdd:COG1340     54 ELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKlRKEIERlewrqQT-EVLSP 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  915 EKEQALadlnsVEKsLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKvhaeEKLDRANAEIAQVR 994
Cdd:COG1340    133 EEEKEL-----VEK-IKELEKELEKAKKALEKNEKLKELRAE-LKELRKEAEEIHKKIKELA----EEAQELHEEMIELY 201

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907183035  995 GKAQqeqaayqaSLRKE-----------QLRVDALERTLEQKNKEIEELTKICDELIAK 1042
Cdd:COG1340    202 KEAD--------ELRKEadelhkeiveaQEKADELHEEIIELQKELRELRKELKKLRKK 252
PRK12704 PRK12704
phosphodiesterase; Provisional
 938-1042 6.46e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 6.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  938 EKMKEVLEGFRKNEEVLKKcaqEYLSRVKKEEQRyqaLKVHAEEKLDRANAEIAQVRGKAQQEQAA---YQASLRKEQLR 1014
Cdd:PRK12704    38 EEAKRILEEAKKEAEAIKK---EALLEAKEEIHK---LRNEFEKELRERRNELQKLEKRLLQKEENldrKLELLEKREEE 111

                           90       100
                   ....*....|....*....|....*...
gi 1907183035 1015 VDALERTLEQKNKEIEELTKICDELIAK 1042
Cdd:PRK12704   112 LEKKEKELEQKQQELEKKEEELEELIEE 139
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
 540-793 6.98e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 40.46  E-value: 6.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  540 PPSQD-PTPAATPEAPSAIST-VVHATDEEKLAVTSQKWTCMTVDLDADKQDFPQPSDlsNFVNETKFNSPSEELDYrnS 617
Cdd:PRK08691   434 PPWEDaPDEAQTAAGTAQTSAkSIQTASEAETPPENQVSKNKAADNETDAPLSEVPSE--NPIQATPNDEAVETETF--A 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  618 YEIEYMEKLGSSLPQDDDTPKKQALYLMFDTPQESPVKSP---------PVRMSDSPTPCSGSSFEDTEalvNAATKLQH 688
Cdd:PRK08691   510 HEAPAEPFYGYGFPDNDCPPEDGAEIPPPDWEHAAPADTAgggadeeaeAGGIGGNNTPSAPPPEFSTE---NWAAIVRH 586

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  689 pVARGLPSSQEPLLQVPEKPSQKELEAMALGTPAEAIEITAPEGAFASADTLLSRLAHPASLcgALGYLEPDLAEKNPPV 768
Cdd:PRK08691   587 -FARKLGAAQMPAQHSAWTEYHPDTGLMVLAMTAEARATADKKRLDKIRDTLAQAYGLQLTL--QTQDWRDEAGRETPAM 663

                          250       260
                   ....*....|....*....|....*.
gi 1907183035  769 FAQKLQ-EELEFAVMRIEALKLARQI 793
Cdd:PRK08691   664 QDKRVQaEDRQKAQALLEADPAAQKI 689
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 888-1033 7.43e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 7.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  888 IAQMIGKPEDEQRE--KSIShqTVQQLVLEKEQALADLNSVEKSLadlfrryEKMKEVLEGFRKNEEVLKK---CAQEYL 962
Cdd:TIGR02169  144 VTDFISMSPVERRKiiDEIA--GVAEFDRKKEKALEELEEVEENI-------ERLDLIIDEKRQQLERLRRereKAERYQ 214

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907183035  963 SRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELT 1033
Cdd:TIGR02169  215 ALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG 285
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
850-1039 9.54e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 9.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  850 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYE-----KTIAQMIGKPE--------DEQREKSISHQTVQQLVLEK 916
Cdd:PRK03918   458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklKELAEQLKELEeklkkynlEELEKKAEEYEKLKEKLIKL 537

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183035  917 EQALADLNSVEKSLADLFRRYEKMKEVLEGF-RKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEiaqvrg 995
Cdd:PRK03918   538 KGEIKSLKKELEKLEELKKKLAELEKKLDELeEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE------ 611

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907183035  996 kaqQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDEL 1039
Cdd:PRK03918   612 ---KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
 
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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