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Conserved domains on  [gi|1720423607|ref|XP_030098694|]
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transforming acidic coiled-coil-containing protein 2 isoform X40 [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 ...
741-944 9.23e-99

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: 308.14  E-value: 9.23e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 741 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIgkpEDEQREKSISHQTVQQLVLEK 820
Cdd:pfam05010   1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMI---EEKQKQKELEHAEIQKVLEEK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 821 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGK 900
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720423607 901 AQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 944
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
PRK13335 super family cl31400
superantigen-like protein SSL3; Reviewed;
183-294 3.06e-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: 43.96  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 183 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 255
Cdd:PRK13335   45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720423607 256 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 294
Cdd:PRK13335  125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
PHA03247 super family cl33720
large tegument protein UL36; Provisional
62-408 9.82e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 9.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607   62 PPAPEEPGCISEPpVVVPDGP--RSSESVEGSPFRPSHSSSAVFDEDKPIASSGTYNLDFDSIELVDNFQSLEPCSADSK 139
Cdd:PHA03247  2561 PAAPDRSVPPPRP-APRPSEPavTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPD 2639
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  140 GQECKVSTRRKSTESVP-PSKSTLSRSLSLQASDFDGASCPGSPEAGTLTtDACGTGSNSAsstlkrtkktRPPSLKKKQ 218
Cdd:PHA03247  2640 PHPPPTVPPPERPRDDPaPGRVSRPRRARRLGRAAQASSPPQRPRRRAAR-PTVGSLTSLA----------DPPPPPPTP 2708
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  219 ATKKPTETP--PVKETQQEPGEESPVPSEEHLAPETKTESATPEGAGCTLSDDTPL-----ESPAVPTATCPLTLeSAED 291
Cdd:PHA03247  2709 EPAPHALVSatPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAgppapAPPAAPAAGPPRRL-TRPA 2787
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  292 VSPLVSGGGRVQNSPPVGRKSVPLTTASEAVEVTLSDSGGQ----EDLPAKGLSVRLEFDYSEDKGSWESQQ---ENAPP 364
Cdd:PHA03247  2788 VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLppptSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRRPP 2867
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1720423607  365 TKKIGKKPVA--KMPLRR---PKMKKTPEKLDNTPASPPRSPTEPSDTP 408
Cdd:PHA03247  2868 SRSPAAKPAApaRPPVRRlarPAVSRSTESFALPPDQPERPPQPQAPPP 2916
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
741-944 9.23e-99

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: 308.14  E-value: 9.23e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 741 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIgkpEDEQREKSISHQTVQQLVLEK 820
Cdd:pfam05010   1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMI---EEKQKQKELEHAEIQKVLEEK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 821 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGK 900
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720423607 901 AQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 944
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
745-946 3.87e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 3.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 745 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQAL 824
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 825 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 904
Cdd:COG1196   330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720423607 905 QAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 946
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
739-938 1.92e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 739 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKT---IAQMigKPEDEQREKSIshQTVQQ 815
Cdd:PRK03918  184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEEL--EKELESLEGSK--RKLEE 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 816 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA--- 892
Cdd:PRK03918  260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkee 338
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 893 --------------EIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTK 938
Cdd:PRK03918  339 rleelkkklkelekRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
745-946 8.12e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 8.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  745 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREksishqtVQQLVLEKEQAL 824
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE-------LTELEAEIEELE 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  825 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 904
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1720423607  905 QAAYQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 946
Cdd:TIGR02168  841 EDLEE---QIEELSED-----IESLAAEIEELEELIEELESE 874
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
183-294 3.06e-04

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 43.96  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 183 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 255
Cdd:PRK13335   45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720423607 256 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 294
Cdd:PRK13335  125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
PHA03247 PHA03247
large tegument protein UL36; Provisional
62-408 9.82e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 9.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607   62 PPAPEEPGCISEPpVVVPDGP--RSSESVEGSPFRPSHSSSAVFDEDKPIASSGTYNLDFDSIELVDNFQSLEPCSADSK 139
Cdd:PHA03247  2561 PAAPDRSVPPPRP-APRPSEPavTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPD 2639
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  140 GQECKVSTRRKSTESVP-PSKSTLSRSLSLQASDFDGASCPGSPEAGTLTtDACGTGSNSAsstlkrtkktRPPSLKKKQ 218
Cdd:PHA03247  2640 PHPPPTVPPPERPRDDPaPGRVSRPRRARRLGRAAQASSPPQRPRRRAAR-PTVGSLTSLA----------DPPPPPPTP 2708
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  219 ATKKPTETP--PVKETQQEPGEESPVPSEEHLAPETKTESATPEGAGCTLSDDTPL-----ESPAVPTATCPLTLeSAED 291
Cdd:PHA03247  2709 EPAPHALVSatPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAgppapAPPAAPAAGPPRRL-TRPA 2787
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  292 VSPLVSGGGRVQNSPPVGRKSVPLTTASEAVEVTLSDSGGQ----EDLPAKGLSVRLEFDYSEDKGSWESQQ---ENAPP 364
Cdd:PHA03247  2788 VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLppptSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRRPP 2867
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1720423607  365 TKKIGKKPVA--KMPLRR---PKMKKTPEKLDNTPASPPRSPTEPSDTP 408
Cdd:PHA03247  2868 SRSPAAKPAApaRPPVRRlarPAVSRSTESFALPPDQPERPPQPQAPPP 2916
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
741-944 9.23e-99

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: 308.14  E-value: 9.23e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 741 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIgkpEDEQREKSISHQTVQQLVLEK 820
Cdd:pfam05010   1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMI---EEKQKQKELEHAEIQKVLEEK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 821 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGK 900
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720423607 901 AQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 944
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
745-946 3.87e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 3.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 745 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQAL 824
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 825 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 904
Cdd:COG1196   330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720423607 905 QAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 946
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
739-938 1.92e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 739 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKT---IAQMigKPEDEQREKSIshQTVQQ 815
Cdd:PRK03918  184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEEL--EKELESLEGSK--RKLEE 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 816 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA--- 892
Cdd:PRK03918  260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkee 338
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 893 --------------EIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTK 938
Cdd:PRK03918  339 rleelkkklkelekRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
800-947 2.84e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 2.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 800 EDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADL---FRRYEKMKEVLEGFRKNEEvLKKCAQEYLSRVKKEEQRY 876
Cdd:COG4717    77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeLEKLEKLLQLLPLYQELEA-LEAELAELPERLEELEERL 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 877 QALKvHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKE-----------QLRVDALERTLEQKNKEIEELTKICDELIA 945
Cdd:COG4717   156 EELR-ELEEELEELEAELAELQEELEELLEQLSLATEEElqdlaeeleelQQRLAELEEELEEAQEELEELEEELEQLEN 234

                  ..
gi 1720423607 946 KM 947
Cdd:COG4717   235 EL 236
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
742-946 7.91e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 49.38  E-value: 7.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 742 QQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIaqmigkpedEQREKSISHQTVQQLVLEKE 821
Cdd:COG4942    49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---------EAQKEELAELLRALYRLGRQ 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 822 QALADLNSVEkSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKA 901
Cdd:COG4942   120 PPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720423607 902 QQEqaayqasLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 946
Cdd:COG4942   198 QKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAE 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
745-946 8.12e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 8.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  745 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREksishqtVQQLVLEKEQAL 824
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE-------LTELEAEIEELE 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  825 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 904
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1720423607  905 QAAYQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 946
Cdd:TIGR02168  841 EDLEE---QIEELSED-----IESLAAEIEELEELIEELESE 874
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
736-938 2.29e-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: 48.51  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  736 PPGLLFQQPDLDSALQVARAEVIAK-EREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQ 814
Cdd:TIGR02168  657 PGGVITGGSAKTNSSILERRREIEElEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  815 QLVLEKEQALADLNSVEKSLADLfrrYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANAEI 894
Cdd:TIGR02168  737 RLEAEVEQLEERIAQLSKELTEL---EAEIEELEERLEEAEEELAEAEAE-IEELEAQIEQLKEELKALREALDELRAEL 812
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1720423607  895 AQVRGKAQQEQAAYQASLRK---EQLRVDALERTLEQKNKEIEELTK 938
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRiaaTERRLEDLEEQIEELSEDIESLAA 859
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
742-929 2.66e-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: 2.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  742 QQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREksisHQTVQQLVLEKE 821
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ----LETLRSKVAQLE 392
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  822 QALADLNS----VEKSLADLFRRYEKMKEVLEGFRKN-EEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQ 896
Cdd:TIGR02168  393 LQIASLNNeierLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1720423607  897 VRgkaqQEQAAYQASLRKEQLRVDALERTLEQK 929
Cdd:TIGR02168  473 AE----QALDAAERELAQLQARLDSLERLQENL 501
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
752-945 2.80e-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: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  752 VARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIA---QMIGKPEDEqREKSISHQTVQQ---------LVLE 819
Cdd:TIGR02169  153 VERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDekrQQLERLRRE-REKAERYQALLKekreyegyeLLKE 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  820 KEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKE-EQRYQALKvhaeEKLDRANAEIAQVR 898
Cdd:TIGR02169  232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVK----EKIGELEAEIASLE 307
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720423607  899 GKAQQEQAAYQAS---LRKEQLRVDALERTLEQKNKEIEELTKICDELIA 945
Cdd:TIGR02169  308 RSIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
735-938 2.98e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 735 KPPGLLFQQPDLDSALQVARAEV---IAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAqmigkpedeqreksishq 811
Cdd:COG4717    65 KPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQ------------------ 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 812 tVQQLVLEKEQAladlnsvEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRAN 891
Cdd:COG4717   127 -LLPLYQELEAL-------EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720423607 892 AEIAQVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEIEELTK 938
Cdd:COG4717   199 EELEELQQR-----------LAELEEELEEAQEELEELEEELEQLEN 234
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
777-936 3.00e-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: 3.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  777 EVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVL---EKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRK 853
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLevsELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  854 NEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEI 933
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-----------LEELEAELEELESRLEELEEQL 381

                   ...
gi 1720423607  934 EEL 936
Cdd:TIGR02168  382 ETL 384
PTZ00121 PTZ00121
MAEBL; Provisional
754-938 9.69e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 9.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  754 RAEVIAKERE----VSEWRDKYEESRREVVEMRKiVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALADLNS 829
Cdd:PTZ00121  1621 KAEELKKAEEekkkVEQLKKKEAEEKKKAEELKK-AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  830 VEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKldranAEIAQVrgKAQQEQAAYQ 909
Cdd:PTZ00121  1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK-----KKIAHL--KKEEEKKAEE 1772
                          170       180
                   ....*....|....*....|....*....
gi 1720423607  910 ASLRKEQLRVDALERTLEQKNKEIEELTK 938
Cdd:PTZ00121  1773 IRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
PTZ00121 PTZ00121
MAEBL; Provisional
745-938 2.33e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  745 DLDSALQVARAEVIAKEREV--SEWRDKYEESRREvvEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQT---VQQLVLE 819
Cdd:PTZ00121  1538 EAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmkAEEAKKA 1615
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  820 KE-----QALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANA-- 892
Cdd:PTZ00121  1616 EEakikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlk 1695
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720423607  893 -------EIAQVRgKAQQEQAAYQASLRKEQ----LRVDALERTLEQKNKEIEELTK 938
Cdd:PTZ00121  1696 keaeeakKAEELK-KKEAEEKKKAEELKKAEeenkIKAEEAKKEAEEDKKKAEEAKK 1751
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
183-294 3.06e-04

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 43.96  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 183 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 255
Cdd:PRK13335   45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720423607 256 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 294
Cdd:PRK13335  125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
746-944 1.01e-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: 43.13  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  746 LDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQT-----------VQ 814
Cdd:TIGR02169  228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkigeleaeiasLE 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  815 QLVLEKEQALADLnsvEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEkLDRANAEi 894
Cdd:TIGR02169  308 RSIAEKERELEDA---EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE-VDKEFAE- 382
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720423607  895 aqvrgkaqqeqaayqasLRKEQlrvDALERTLEQKNKEIEELTKICDELI 944
Cdd:TIGR02169  383 -----------------TRDEL---KDYREKLEKLKREINELKRELDRLQ 412
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
761-949 1.44e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 761 EREVSEWRDKYEESRREVVEMRKIVAEYE--KTIAQMIGKPEDEQREKSIshqtvqqlvleKEQALADLNSVEKSLADLF 838
Cdd:PRK03918  404 EEEISKITARIGELKKEIKELKKAIEELKkaKGKCPVCGRELTEEHRKEL-----------LEEYTAELKRIEKELKEIE 472
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 839 RRYEKMKEV---LEGFRKNEEVLKKcAQEYLSRVKKEEQRyqaLKVHAEEKLDRANAEIAQVRGKAQQEQAAYQaSLRKE 915
Cdd:PRK03918  473 EKERKLRKElreLEKVLKKESELIK-LKELAEQLKELEEK---LKKYNLEELEKKAEEYEKLKEKLIKLKGEIK-SLKKE 547
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1720423607 916 QLRVDALERTLEQKNKEIEELTKICDELIAKMGK 949
Cdd:PRK03918  548 LEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
757-945 1.65e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 757 VIAKEREVSEWRDKYE-----ESRREVVEMRKIVA---EYEKTIAQMIG-KPEDEQREKSISHqtVQQLVLEKEQALADL 827
Cdd:PRK03918  488 VLKKESELIKLKELAEqlkelEEKLKKYNLEELEKkaeEYEKLKEKLIKlKGEIKSLKKELEK--LEELKKKLAELEKKL 565
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 828 NSVEKSLADLFRRYEKmkevlEGFRKNEEV------LKKCAQEYL------SRVKKEEQRYQALK---VHAEEKLDRANA 892
Cdd:PRK03918  566 DELEEELAELLKELEE-----LGFESVEELeerlkeLEPFYNEYLelkdaeKELEREEKELKKLEeelDKAFEELAETEK 640
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720423607 893 EIAQVRGK----AQQEQAAYQASLRKEQLRvdaLERTLEQKNKEIEELTKICDELIA 945
Cdd:PRK03918  641 RLEELRKEleelEKKYSEEEYEELREEYLE---LSRELAGLRAELEELEKRREEIKK 694
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
745-932 1.70e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 745 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQAL 824
Cdd:COG4942    59 ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 825 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRgKAQQE 904
Cdd:COG4942   139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAE 217
                         170       180
                  ....*....|....*....|....*...
gi 1720423607 905 QAAYQASLRKEqlrVDALERTLEQKNKE 932
Cdd:COG4942   218 LQQEAEELEAL---IARLEAEAAAAAER 242
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
745-949 1.72e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 745 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQAL 824
Cdd:COG4372    63 QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 825 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKcaQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 904
Cdd:COG4372   143 SEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEEL 220
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720423607 905 QAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGK 949
Cdd:COG4372   221 LEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
813-937 2.64e-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: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  813 VQQLVLEKEQALADLNsvekSLADLFRRYEKMKEVLEGFRKNEEVL---KKCAQEYLS-RVKKEEQRYQALKVH---AEE 885
Cdd:COG4913    213 VREYMLEEPDTFEAAD----ALVEHFDDLERAHEALEDAREQIELLepiRELAERYAAaRERLAELEYLRAALRlwfAQR 288
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720423607  886 KLDRANAEIAQVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEIEELT 937
Cdd:COG4913    289 RLELLEAELEELRAE-----------LARLEAELERLEARLDALREELDELE 329
PTZ00121 PTZ00121
MAEBL; Provisional
759-946 2.77e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  759 AKEREVSEWRDKYEESRREVVEMRKIVAEYEKtiAQMIGKPEDEQREKSishQTVQQLVLEKEQALADLNSVEKSLADLF 838
Cdd:PTZ00121  1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK--ADEAKKKAEEAKKKA---DEAKKAAEAKKKADEAKKAEEAKKADEA 1527
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  839 RRYEKMKEVLEgFRKNEEVLKKCAQEYLSRVKK-EEQRYQALKVHAEEKLDRA--NAEIA----QVRGKAQQEQAAYQAS 911
Cdd:PTZ00121  1528 KKAEEAKKADE-AKKAEEKKKADELKKAEELKKaEEKKKAEEAKKAEEDKNMAlrKAEEAkkaeEARIEEVMKLYEEEKK 1606
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1720423607  912 LRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 946
Cdd:PTZ00121  1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
PRK12704 PRK12704
phosphodiesterase; Provisional
842-946 5.34e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 842 EKMKEVLEGFRKNEEVLKKcaqEYLSRVKKEEQRyqaLKVHAEEKLDRANAEIAQVRGKAQQEQAA---YQASLRKEQLR 918
Cdd:PRK12704   38 EEAKRILEEAKKEAEAIKK---EALLEAKEEIHK---LRNEFEKELRERRNELQKLEKRLLQKEENldrKLELLEKREEE 111
                          90       100
                  ....*....|....*....|....*...
gi 1720423607 919 VDALERTLEQKNKEIEELTKICDELIAK 946
Cdd:PRK12704  112 LEKKEKELEQKQQELEKKEEELEELIEE 139
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
745-946 5.83e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 745 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQR-EKSISH-----QTvQQLVL 818
Cdd:COG1340    54 ELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKlRKEIERlewrqQT-EVLSP 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607 819 EKEQALadlnsVEKsLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKvhaeEKLDRANAEIAQVR 898
Cdd:COG1340   133 EEEKEL-----VEK-IKELEKELEKAKKALEKNEKLKELRAE-LKELRKEAEEIHKKIKELA----EEAQELHEEMIELY 201
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720423607 899 GKAQqeqaayqaSLRKE-----------QLRVDALERTLEQKNKEIEELTKICDELIAK 946
Cdd:COG1340   202 KEAD--------ELRKEadelhkeiveaQEKADELHEEIIELQKELRELRKELKKLRKK 252
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
792-937 6.30e-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: 6.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  792 IAQMIGKPEDEQRE--KSIShqTVQQLVLEKEQALADLNSVEKSLadlfrryEKMKEVLEGFRKNEEVLKK---CAQEYL 866
Cdd:TIGR02169  144 VTDFISMSPVERRKiiDEIA--GVAEFDRKKEKALEELEEVEENI-------ERLDLIIDEKRQQLERLRRereKAERYQ 214
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720423607  867 SRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELT 937
Cdd:TIGR02169  215 ALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG 285
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
749-947 7.29e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 7.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  749 ALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTiaqmigkpeDEQREKSISHQTVQQLVLEKEQALADLN 828
Cdd:COG4913    611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRL---------AEYSWDEIDVASAEREIAELEAELERLD 681
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  829 SVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKcaqeylsRVKKEEQRYQAlkvhAEEKLDRAnAEIAQVRGKAQQEQAAY 908
Cdd:COG4913    682 ASSDDLAALEEQLEELEAELEELEEELDELKG-------EIGRLEKELEQ----AEEELDEL-QDRLEAAEDLARLELRA 749
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1720423607  909 QASLRKEQLRVDALERTL-----EQKNKEIEELTKICDELIAKM 947
Cdd:COG4913    750 LLEERFAAALGDAVERELrenleERIDALRARLNRAEEELERAM 793
PHA03247 PHA03247
large tegument protein UL36; Provisional
62-408 9.82e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 9.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607   62 PPAPEEPGCISEPpVVVPDGP--RSSESVEGSPFRPSHSSSAVFDEDKPIASSGTYNLDFDSIELVDNFQSLEPCSADSK 139
Cdd:PHA03247  2561 PAAPDRSVPPPRP-APRPSEPavTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPD 2639
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  140 GQECKVSTRRKSTESVP-PSKSTLSRSLSLQASDFDGASCPGSPEAGTLTtDACGTGSNSAsstlkrtkktRPPSLKKKQ 218
Cdd:PHA03247  2640 PHPPPTVPPPERPRDDPaPGRVSRPRRARRLGRAAQASSPPQRPRRRAAR-PTVGSLTSLA----------DPPPPPPTP 2708
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  219 ATKKPTETP--PVKETQQEPGEESPVPSEEHLAPETKTESATPEGAGCTLSDDTPL-----ESPAVPTATCPLTLeSAED 291
Cdd:PHA03247  2709 EPAPHALVSatPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAgppapAPPAAPAAGPPRRL-TRPA 2787
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423607  292 VSPLVSGGGRVQNSPPVGRKSVPLTTASEAVEVTLSDSGGQ----EDLPAKGLSVRLEFDYSEDKGSWESQQ---ENAPP 364
Cdd:PHA03247  2788 VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLppptSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRRPP 2867
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1720423607  365 TKKIGKKPVA--KMPLRR---PKMKKTPEKLDNTPASPPRSPTEPSDTP 408
Cdd:PHA03247  2868 SRSPAAKPAApaRPPVRRlarPAVSRSTESFALPPDQPERPPQPQAPPP 2916
 
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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