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Conserved domains on  [gi|1039779420|ref|XP_017177887|]
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transforming acidic coiled-coil-containing protein 2 isoform X10 [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 ...
2685-2888 6.00e-103

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: 328.56  E-value: 6.00e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2685 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIgkpEDEQREKSISHQTVQQLVLEK 2764
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMI---EEKQKQKELEHAEIQKVLEEK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2765 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGK 2844
Cdd:pfam05010   78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1039779420 2845 AQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 2888
Cdd:pfam05010  158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
PRK13335 super family cl31400
superantigen-like protein SSL3; Reviewed;
2019-2130 2.42e-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: 46.27  E-value: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2019 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 2091
Cdd:PRK13335    45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1039779420 2092 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 2130
Cdd:PRK13335   125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
2685-2888 6.00e-103

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: 328.56  E-value: 6.00e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2685 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIgkpEDEQREKSISHQTVQQLVLEK 2764
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMI---EEKQKQKELEHAEIQKVLEEK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2765 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGK 2844
Cdd:pfam05010   78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1039779420 2845 AQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 2888
Cdd:pfam05010  158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2610-2890 3.25e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 3.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2610 AEKnppvfAQKLQEELEfaVMRIEALKLARQIALASRSRQDTKREAahppdvsisktalysrigstevekppgllfqqpd 2689
Cdd:COG1196    212 AER-----YRELKEELK--ELEAELLLLKLRELEAELEELEAELEE---------------------------------- 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2690 LDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALA 2769
Cdd:COG1196    251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2770 DLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQ 2849
Cdd:COG1196    331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1039779420 2850 AAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 2890
Cdd:COG1196    411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2683-2892 4.67e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.92  E-value: 4.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2683 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKT---IAQMigKPEDEQREKSIshQTVQQ 2759
Cdd:PRK03918   184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEEL--EKELESLEGSK--RKLEE 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2760 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA--- 2836
Cdd:PRK03918   260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkee 338
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779420 2837 --------------EIAQVRGKAQQEQAAYQASLRKEQLR-------VDALERTLEQKNKEIEELTKICDELIAKMG 2892
Cdd:PRK03918   339 rleelkkklkelekRLEELEERHELYEEAKAKKEELERLKkrltgltPEKLEKELEELEKAKEEIEEEISKITARIG 415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2689-2890 8.86e-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: 51.60  E-value: 8.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2689 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREksishqtVQQLVLEKEQAL 2768
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE-------LTELEAEIEELE 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2769 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 2848
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1039779420 2849 QAAYQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 2890
Cdd:TIGR02168  841 EDLEE---QIEELSED-----IESLAAEIEELEELIEELESE 874
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
2019-2130 2.42e-04

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 46.27  E-value: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2019 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 2091
Cdd:PRK13335    45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1039779420 2092 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 2130
Cdd:PRK13335   125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
2685-2888 6.00e-103

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: 328.56  E-value: 6.00e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2685 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIgkpEDEQREKSISHQTVQQLVLEK 2764
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMI---EEKQKQKELEHAEIQKVLEEK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2765 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGK 2844
Cdd:pfam05010   78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1039779420 2845 AQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 2888
Cdd:pfam05010  158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2610-2890 3.25e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 3.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2610 AEKnppvfAQKLQEELEfaVMRIEALKLARQIALASRSRQDTKREAahppdvsisktalysrigstevekppgllfqqpd 2689
Cdd:COG1196    212 AER-----YRELKEELK--ELEAELLLLKLRELEAELEELEAELEE---------------------------------- 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2690 LDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALA 2769
Cdd:COG1196    251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2770 DLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQ 2849
Cdd:COG1196    331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1039779420 2850 AAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 2890
Cdd:COG1196    411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2683-2892 4.67e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.92  E-value: 4.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2683 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKT---IAQMigKPEDEQREKSIshQTVQQ 2759
Cdd:PRK03918   184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEEL--EKELESLEGSK--RKLEE 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2760 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA--- 2836
Cdd:PRK03918   260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkee 338
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779420 2837 --------------EIAQVRGKAQQEQAAYQASLRKEQLR-------VDALERTLEQKNKEIEELTKICDELIAKMG 2892
Cdd:PRK03918   339 rleelkkklkelekRLEELEERHELYEEAKAKKEELERLKkrltgltPEKLEKELEELEKAKEEIEEEISKITARIG 415
PTZ00121 PTZ00121
MAEBL; Provisional
2629-2882 9.48e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 9.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2629 VMRIEALKLARQIALASRSRQDTKREAAHPPDVSISKTALYSRIGSTEVEKPPGLLFQQPDLDSALQV-ARAEVIAKERE 2707
Cdd:PTZ00121  1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEE 1630
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2708 ----VSEWRDKYEESRREVVEMRKiVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFR 2783
Cdd:PTZ00121  1631 ekkkVEQLKKKEAEEKKKAEELKK-AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2784 RYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKldranAEIAQVrgKAQQEQAAYQASLRKEQLRV 2863
Cdd:PTZ00121  1710 KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK-----KKIAHL--KKEEEKKAEEIRKEKEAVIE 1782
                          250
                   ....*....|....*....
gi 1039779420 2864 DALERTLEQKNKEIEELTK 2882
Cdd:PTZ00121  1783 EELDEEDEKRRMEVDKKIK 1801
PTZ00121 PTZ00121
MAEBL; Provisional
2693-2890 1.49e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 1.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2693 ALQVARAEVIAKErevSEWRDKYEESRREVVEMRKivAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALAD-- 2770
Cdd:PTZ00121  1453 AEEAKKAEEAKKK---AEEAKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADea 1527
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2771 LNSVEKSLADLFRRYEKMKEVLEgFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQA 2850
Cdd:PTZ00121  1528 KKAEEAKKADEAKKAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1039779420 2851 AYQASLRK-EQLRVDALE-RTLEQKNKEIEELTKICDELIAK 2890
Cdd:PTZ00121  1607 MKAEEAKKaEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKK 1648
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2744-2891 3.95e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 3.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2744 EDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADL---FRRYEKMKEVLEGFRKNEEvLKKCAQEYLSRVKKEEQRY 2820
Cdd:COG4717     77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeLEKLEKLLQLLPLYQELEA-LEAELAELPERLEELEERL 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2821 QALKvHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKE-----------QLRVDALERTLEQKNKEIEELTKICDELIA 2889
Cdd:COG4717    156 EELR-ELEEELEELEAELAELQEELEELLEQLSLATEEElqdlaeeleelQQRLAELEEELEEAQEELEELEEELEQLEN 234

                   ..
gi 1039779420 2890 KM 2891
Cdd:COG4717    235 EL 236
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2689-2890 8.86e-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: 51.60  E-value: 8.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2689 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREksishqtVQQLVLEKEQAL 2768
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE-------LTELEAEIEELE 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2769 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 2848
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1039779420 2849 QAAYQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 2890
Cdd:TIGR02168  841 EDLEE---QIEELSED-----IESLAAEIEELEELIEELESE 874
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2696-2889 9.46e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 9.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2696 VARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIA---QMIGKPEDEqREKSISHQTVQQ---------LVLE 2763
Cdd:TIGR02169  153 VERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDekrQQLERLRRE-REKAERYQALLKekreyegyeLLKE 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2764 KEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKE-EQRYQALKvhaeEKLDRANAEIAQVR 2842
Cdd:TIGR02169  232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVK----EKIGELEAEIASLE 307
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2843 GKAQQEQAAYQAS---LRKEQLRVDALERTLEQKNKEIEELTKICDELIA 2889
Cdd:TIGR02169  308 RSIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2690-2889 1.61e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 1.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2690 LDSALQVARAE------VIAKEREVSEWRDKYE-----ESRREVVEMRKIVA---EYEKTIAQMIG-KPEDEQREKSISH 2754
Cdd:PRK03918   471 IEEKERKLRKElrelekVLKKESELIKLKELAEqlkelEEKLKKYNLEELEKkaeEYEKLKEKLIKlKGEIKSLKKELEK 550
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2755 qtVQQLVLEKEQALADLNSVEKSLADLFRRYEKmkevlEGFRKNEEV------LKKCAQEYL------SRVKKEEQRYQA 2822
Cdd:PRK03918   551 --LEELKKKLAELEKKLDELEEELAELLKELEE-----LGFESVEELeerlkeLEPFYNEYLelkdaeKELEREEKELKK 623
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779420 2823 LK---VHAEEKLDRANAEIAQVRGK----AQQEQAAYQASLRKEQLRvdaLERTLEQKNKEIEELTKICDELIA 2889
Cdd:PRK03918   624 LEeelDKAFEELAETEKRLEELRKEleelEKKYSEEEYEELREEYLE---LSRELAGLRAELEELEKRREEIKK 694
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
2689-2890 2.06e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 49.14  E-value: 2.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2689 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQR-EKSISH-----QTvQQLVL 2762
Cdd:COG1340     54 ELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKlRKEIERlewrqQT-EVLSP 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2763 EKEQALadlnsVEKsLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEylsRVKKEEQRyQALKVHAEEkLDRANAEIAQVR 2842
Cdd:COG1340    133 EEEKEL-----VEK-IKELEKELEKAKKALEKNEKLKELRAELKEL---RKEAEEIH-KKIKELAEE-AQELHEEMIELY 201
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779420 2843 GKAQqeqaayqaSLRKE-----------QLRVDALERTLEQKNKEIEELTKICDELIAK 2890
Cdd:COG1340    202 KEAD--------ELRKEadelhkeiveaQEKADELHEEIIELQKELRELRKELKKLRKK 252
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2680-2882 2.58e-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: 50.06  E-value: 2.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2680 PPGLLFQQPDLDSALQVARAEVIAK-EREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQ 2758
Cdd:TIGR02168  657 PGGVITGGSAKTNSSILERRREIEElEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2759 QLVLEKEQALADLNSVEKSLADLfrrYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANAEI 2838
Cdd:TIGR02168  737 RLEAEVEQLEERIAQLSKELTEL---EAEIEELEERLEEAEEELAEAEAE-IEELEAQIEQLKEELKALREALDELRAEL 812
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1039779420 2839 AQVRGKAQQEQAAYQASLRK---EQLRVDALERTLEQKNKEIEELTK 2882
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRiaaTERRLEDLEEQIEELSEDIESLAA 859
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2686-2890 2.95e-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: 48.99  E-value: 2.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2686 QQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIaqmigkpedEQREKSISHQTVQQLVLEKE 2765
Cdd:COG4942     49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---------EAQKEELAELLRALYRLGRQ 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2766 QALADLNSVEkSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKA 2845
Cdd:COG4942    120 PPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1039779420 2846 QQEqaayqasLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 2890
Cdd:COG4942    198 QKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAE 235
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2620-2893 3.16e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 3.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2620 KLQEELEFAVMRIE--ALKLARQIALASRSRQDTKREAAHPPDvsisktalysrigstEVEKppgllfqqpDLDSaLQVA 2697
Cdd:PRK03918   345 KKLKELEKRLEELEerHELYEEAKAKKEELERLKKRLTGLTPE---------------KLEK---------ELEE-LEKA 399
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2698 RAEViakEREVSEWRDKYEESRREVVEMRKIVAEYE--KTIAQMIGKPEDEQREKSIshqtvqqlvleKEQALADLNSVE 2775
Cdd:PRK03918   400 KEEI---EEEISKITARIGELKKEIKELKKAIEELKkaKGKCPVCGRELTEEHRKEL-----------LEEYTAELKRIE 465
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2776 KSLADLFRRYEKMKEV---LEGFRKNEEVLKKcAQEYLSRVKKEEQRyqaLKVHAEEKLDRANAEIAQVRGKAQQEQAAY 2852
Cdd:PRK03918   466 KELKEIEEKERKLRKElreLEKVLKKESELIK-LKELAEQLKELEEK---LKKYNLEELEKKAEEYEKLKEKLIKLKGEI 541
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1039779420 2853 QaSLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGK 2893
Cdd:PRK03918   542 K-SLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2686-2873 3.27e-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: 3.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2686 QQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREksisHQTVQQLVLEKE 2765
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ----LETLRSKVAQLE 392
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2766 QALADLNS----VEKSLADLFRRYEKMKEVLEGFRKN-EEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQ 2840
Cdd:TIGR02168  393 LQIASLNNeierLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1039779420 2841 VRgkaqQEQAAYQASLRKEQLRVDALERTLEQK 2873
Cdd:TIGR02168  473 AE----QALDAAERELAQLQARLDSLERLQENL 501
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2679-2882 3.63e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 3.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2679 KPPGLLFQQPDLDSALQVARAEV---IAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAqmigkpedeqreksishq 2755
Cdd:COG4717     65 KPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQ------------------ 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2756 tVQQLVLEKEQAladlnsvEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRAN 2835
Cdd:COG4717    127 -LLPLYQELEAL-------EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1039779420 2836 AEIAQVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEIEELTK 2882
Cdd:COG4717    199 EELEELQQR-----------LAELEEELEEAQEELEELEEELEQLEN 234
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2721-2880 4.01e-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: 4.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2721 EVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVL---EKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRK 2797
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLevsELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2798 NEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEI 2877
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-----------LEELEAELEELESRLEELEEQL 381

                   ...
gi 1039779420 2878 EEL 2880
Cdd:TIGR02168  382 ETL 384
PTZ00121 PTZ00121
MAEBL; Provisional
2689-2890 7.92e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 7.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2689 DLDSALQVARAEVIAKEREV--SEWRDKYEESRREvvEMRKIVAEYEKTIAQMIgkpeDEQREKSISHQTVQQLVLEKEQ 2766
Cdd:PTZ00121  1538 EAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKA--EEDKNMALRKAEEAKKA----EEARIEEVMKLYEEEKKMKAEE 1611
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2767 ALADlnSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEylsrVKKEEQRYqalKVHAEEKLDRANAEiaqvRGKAQ 2846
Cdd:PTZ00121  1612 AKKA--EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEEN---KIKAAEEAKKAEED----KKKAE 1678
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1039779420 2847 QEQAAYQASLRKEQlrvdALERTLEQKNKeIEELTKICDELIAK 2890
Cdd:PTZ00121  1679 EAKKAEEDEKKAAE----ALKKEAEEAKK-AEELKKKEAEEKKK 1717
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2619-2888 1.25e-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: 47.76  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2619 QKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAhppdvsISKTALYSRIGSTEVEKppgLLFQQPDLDSALQVAR 2698
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA------ERYQALLKEKREYEGYE---LLKEKEALERQKEAIE 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2699 AEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMigkPEDEQRE--KSISHQTVQQLVLEKEQALADLN--SV 2774
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL---GEEEQLRvkEKIGELEAEIASLERSIAEKEREleDA 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2775 EKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEkLDRANAEiaqvrgkaqqeqaayqa 2854
Cdd:TIGR02169  321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE-VDKEFAE----------------- 382
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1039779420 2855 sLRKEQlrvDALERTLEQKNKEIEELTKICDELI 2888
Cdd:TIGR02169  383 -TRDEL---KDYREKLEKLKREINELKRELDRLQ 412
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2619-2890 2.06e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 2.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2619 QKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAhppdvsisKTALYsrigstevekppgllfqqpDLDSALQVAR 2698
Cdd:COG1196    235 RELEAELEELEAELEELEAELEELEAELAELEAELEEL--------RLELE-------------------ELELELEEAQ 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2699 AEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSL 2778
Cdd:COG1196    288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2779 ADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRG--KAQQEQAAYQASL 2856
Cdd:COG1196    368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEleEEEEEEEEALEEA 447
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1039779420 2857 RKEQLRVDALERTLEQKNKEIEELTKICDELIAK 2890
Cdd:COG1196    448 AEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
2019-2130 2.42e-04

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 46.27  E-value: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2019 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 2091
Cdd:PRK13335    45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1039779420 2092 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 2130
Cdd:PRK13335   125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
PTZ00121 PTZ00121
MAEBL; Provisional
2693-2886 5.11e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 5.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2693 ALQVARAEVIAKEREV--SEWRDKYEESRREVVEMRKivAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALAD 2770
Cdd:PTZ00121  1280 ADELKKAEEKKKADEAkkAEEKKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2771 L--NSVEKSLADLFRRYEKmkevlegfRKNEEVLKKCAQEylsrVKKEEQryqaLKVHAEEklDRANAEiaQVRGKAQQE 2848
Cdd:PTZ00121  1358 EaeAAEEKAEAAEKKKEEA--------KKKADAAKKKAEE----KKKADE----AKKKAEE--DKKKAD--ELKKAAAAK 1417
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1039779420 2849 QAAYQASLRKEQLR-VDALERTLEQKNKEiEELTKICDE 2886
Cdd:PTZ00121  1418 KKADEAKKKAEEKKkADEAKKKAEEAKKA-DEAKKKAEE 1455
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2689-2893 6.93e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 6.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2689 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQAL 2768
Cdd:COG4372     63 QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2769 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKcaQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 2848
Cdd:COG4372    143 SEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEEL 220
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1039779420 2849 QAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGK 2893
Cdd:COG4372    221 LEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
2698-2893 8.14e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.13  E-value: 8.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2698 RAEVIAKEREVSEWRDKYEESRREVVE-MRKIVAEYEKTIAQmIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEK 2776
Cdd:COG1340     31 RDELNEELKELAEKRDELNAQVKELREeAQELREKRDELNEK-VKELKEERDELNEKLNELREELDELRKELAELNKAGG 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2777 SLADLFRRYEKM--------------KEVLEGFRKNEEVLK--KCAQEYLSRVKKEEQRYQALKVHAE----------EK 2830
Cdd:COG1340    110 SIDKLRKEIERLewrqqtevlspeeeKELVEKIKELEKELEkaKKALEKNEKLKELRAELKELRKEAEeihkkikelaEE 189
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039779420 2831 LDRANAEIAQVRGKaqqeqaayQASLRKEqlrVDALERTLEQKNKEIEELTKICDELIAKMGK 2893
Cdd:COG1340    190 AQELHEEMIELYKE--------ADELRKE---ADELHKEIVEAQEKADELHEEIIELQKELRE 241
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2705-2838 1.06e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2705 EREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSI-SHQTVQQLVLEKEQALADL-----------N 2772
Cdd:PRK03918   611 EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeEYEELREEYLELSRELAGLraeleelekrrE 690
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779420 2773 SVEKSLADLFRRYEKMKEVlegfRKNEEVLKKcAQEYLSRVKKEEQRYQAL-KVHAEEKLDRANAEI 2838
Cdd:PRK03918   691 EIKKTLEKLKEELEEREKA----KKELEKLEK-ALERVEELREKVKKYKALlKERALSKVGEIASEI 752
PTZ00121 PTZ00121
MAEBL; Provisional
2689-2890 1.22e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2689 DLDSALQVARAEVIAK---EREVSEWRDKYEESRReVVEMRKIVAEYEKTIAQMIGKPEDEQRE----KSISHQTVQQLV 2761
Cdd:PTZ00121  1282 ELKKAEEKKKADEAKKaeeKKKADEAKKKAEEAKK-ADEAKKKAEEAKKKADAAKKKAEEAKKAaeaaKAEAEAAADEAE 1360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2762 LEKEQALAD--LNSVEKSLAD-LFRRYEKMKEVLEGFRKNEEVLKKCaqEYLSRVKKEEQRYQALKVHAEE--KLDRANA 2836
Cdd:PTZ00121  1361 AAEEKAEAAekKKEEAKKKADaAKKKAEEKKKADEAKKKAEEDKKKA--DELKKAAAAKKKADEAKKKAEEkkKADEAKK 1438
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039779420 2837 EIAQVRgKAQQEQAAYQASLRKEQLRVDALE-RTLEQKNKEIEELTKiCDELIAK 2890
Cdd:PTZ00121  1439 KAEEAK-KADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKK-ADEAKKK 1491
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2698-2887 3.11e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 3.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2698 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAqmiGKPEDEQREKSISHQ--TVQQLVLEKEQALADLNSVE 2775
Cdd:PRK03918   268 IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLD---ELREIEKRLSRLEEEinGIEERIKELEEKEERLEELK 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2776 KSLADLFRRYEKMKEVLEGFRKNEEVL-------KKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 2848
Cdd:PRK03918   345 KKLKELEKRLEELEERHELYEEAKAKKeelerlkKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039779420 2849 QAAYQAsLRK-------------EQLRVDALER-TLEQKN--KEIEELTKICDEL 2887
Cdd:PRK03918   425 KKAIEE-LKKakgkcpvcgreltEEHRKELLEEyTAELKRieKELKEIEEKERKL 478
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2736-2881 3.88e-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: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2736 IAQMIGKPEDEQRE--KSIShqTVQQLVLEKEQALADLNSVEKSLadlfrryEKMKEVLEGFRKNEEVLKK---CAQEYL 2810
Cdd:TIGR02169  144 VTDFISMSPVERRKiiDEIA--GVAEFDRKKEKALEELEEVEENI-------ERLDLIIDEKRQQLERLRRereKAERYQ 214
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779420 2811 SRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELT 2881
Cdd:TIGR02169  215 ALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG 285
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2695-2879 4.51e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2695 QVARAEVIAKEREVSEWRDK-YEESRREvvEMRkiVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVL----------- 2762
Cdd:pfam13868  126 RQLREEIDEFNEEQAEWKELeKEEEREE--DER--ILEYLKEKAEREEEREAEREEIEEEKEREIARLRaqqekaqdeka 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2763 EKEQALADLNSVE-------KSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYlsRVKKEEQRYQALKVHAE-EKLDRA 2834
Cdd:pfam13868  202 ERDELRAKLYQEEqerkerqKEREEAEKKARQRQELQQAREEQIELKERRLAEE--AEREEEEFERMLRKQAEdEEIEQE 279
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1039779420 2835 NAEiaQVRGKAQQEQAAYQASLR-KEQLRVDALERTLEQKNKEIEE 2879
Cdd:pfam13868  280 EAE--KRRMKRLEHRRELEKQIEeREEQRAAEREEELEEGERLREE 323
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2618-2876 4.75e-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: 42.06  E-value: 4.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2618 AQKLQEELEfavmriealKLARQIALASRSRQDTKREAAhppdvsisktalysrigstevekppGLLFQQPDLDSALQVA 2697
Cdd:COG4942     22 AAEAEAELE---------QLQQEIAELEKELAALKKEEK-------------------------ALLKQLAALERRIAAL 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2698 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEKS 2777
Cdd:COG4942     68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2778 LADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRgKAQQEQAAYQASLR 2857
Cdd:COG4942    148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELE 226
                          250
                   ....*....|....*....
gi 1039779420 2858 KEqlrVDALERTLEQKNKE 2876
Cdd:COG4942    227 AL---IARLEAEAAAAAER 242
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2757-2881 7.31e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 7.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779420 2757 VQQLVLEKEQALADLNsvekSLADLFRRYEKMKEVLEGFRKNEEVL---KKCAQEYLS-RVKKEEQRYQALKVH---AEE 2829
Cdd:COG4913    213 VREYMLEEPDTFEAAD----ALVEHFDDLERAHEALEDAREQIELLepiRELAERYAAaRERLAELEYLRAALRlwfAQR 288
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039779420 2830 KLDRANAEIAQVRgkaqqeqaayqASLRKEQLRVDALERTLEQKNKEIEELT 2881
Cdd:COG4913    289 RLELLEAELEELR-----------AELARLEAELERLEARLDALREELDELE 329
 
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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