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Conserved domains on  [gi|52486843|ref|NP_001004468|]
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transforming acidic coiled-coil-containing protein 2 isoform c [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 ...
 2673-2873 1.37e-104

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: 333.18  E-value: 1.37e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2673 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQA 2752
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2753 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 2832
Cdd:pfam05010   81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 52486843   2833 EQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 2873
Cdd:pfam05010  161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
PRK13335 super family cl31400
superantigen-like protein SSL3; Reviewed;
2000-2111 2.19e-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: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2000 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 2072
Cdd:PRK13335   45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 52486843  2073 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 2111
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 ...
 2673-2873 1.37e-104

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: 333.18  E-value: 1.37e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2673 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQA 2752
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2753 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 2832
Cdd:pfam05010   81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 52486843   2833 EQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 2873
Cdd:pfam05010  161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2598-2874 2.92e-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: 2.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2598 AEKnppvfAQKLQEELEfaVMRIEALKLARQIALASRSRQDTKREAahppdvsisktalysrigstevekppgllfqqpd 2677
Cdd:COG1196  212 AER-----YRELKEELK--ELEAELLLLKLRELEAELEELEAELEE---------------------------------- 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2678 LDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKsishQTVQQLVLEKEQALADLN 2757
Cdd:COG1196  251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEELA 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2758 SVEKSLADLfrrYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAY 2837
Cdd:COG1196  327 ELEEELEEL---EEELEELEEELEEAEEELEEAEAE-LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 52486843 2838 QASLRKEQLRVDALERTLEQKNKEIEELTKICDELIA 2874
Cdd:COG1196  403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2671-2877 3.48e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 59.31  E-value: 3.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2671 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKT---IAQM-IEDEQREKSIshQTVQQLV 2746
Cdd:PRK03918  184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEELeKELESLEGSK--RKLEEKI 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2747 LEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA----- 2821
Cdd:PRK03918  262 RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkeerl 340

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52486843  2822 ------------EIAQVRGKAQQEQAAYQASLRKEQLR-------VDALERTLEQKNKEIEELTKICDELIAKMG 2877
Cdd:PRK03918  341 eelkkklkelekRLEELEERHELYEEAKAKKEELERLKkrltgltPEKLEKELEELEKAKEEIEEEISKITARIG 415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2677-2875 1.82e-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: 53.91  E-value: 1.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2677 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREksisHQTVQQLVLEKEQALADL 2756
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL----SKELTELEAEIEELEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2757 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2836
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 52486843   2837 YQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 2875
Cdd:TIGR02168  844 EE---QIEELSED-----IESLAAEIEELEELIEELESE 874
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
2000-2111 2.19e-04

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 46.27  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2000 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 2072
Cdd:PRK13335   45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 52486843  2073 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 2111
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 ...
 2673-2873 1.37e-104

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: 333.18  E-value: 1.37e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2673 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQA 2752
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2753 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 2832
Cdd:pfam05010   81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 52486843   2833 EQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 2873
Cdd:pfam05010  161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2598-2874 2.92e-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: 2.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2598 AEKnppvfAQKLQEELEfaVMRIEALKLARQIALASRSRQDTKREAahppdvsisktalysrigstevekppgllfqqpd 2677
Cdd:COG1196  212 AER-----YRELKEELK--ELEAELLLLKLRELEAELEELEAELEE---------------------------------- 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2678 LDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKsishQTVQQLVLEKEQALADLN 2757
Cdd:COG1196  251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEELA 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2758 SVEKSLADLfrrYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAY 2837
Cdd:COG1196  327 ELEEELEEL---EEELEELEEELEEAEEELEEAEAE-LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 52486843 2838 QASLRKEQLRVDALERTLEQKNKEIEELTKICDELIA 2874
Cdd:COG1196  403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2671-2877 3.48e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 59.31  E-value: 3.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2671 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKT---IAQM-IEDEQREKSIshQTVQQLV 2746
Cdd:PRK03918  184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEELeKELESLEGSK--RKLEEKI 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2747 LEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA----- 2821
Cdd:PRK03918  262 RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkeerl 340

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52486843  2822 ------------EIAQVRGKAQQEQAAYQASLRKEQLR-------VDALERTLEQKNKEIEELTKICDELIAKMG 2877
Cdd:PRK03918  341 eelkkklkelekRLEELEERHELYEEAKAKKEELERLKkrltgltPEKLEKELEELEKAKEEIEEEISKITARIG 415
PTZ00121 PTZ00121
MAEBL; Provisional
 2617-2867 1.32e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2617 VMRIEALKLARQIALASRSRQDTKREAAHPPDVSISKTALYSRIgsTEVEKppglLFQQPDLDSALQVARAEviaKEREV 2696
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI--EEVMK----LYEEEKKMKAEEAKKAE---EAKIK 1621

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2697 SEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQA--LADLNSVEKSLADLFRRYEKMK 2774
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEA 1701

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2775 EVLEGFRKNEEVLKKCAQEYlsRVKKEEQRYQALKVHAEEKLDRANAEIAQVR-------GKAQQEQAAYQASLRKEQLR 2847
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEEL--KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeekkkiAHLKKEEEKKAEEIRKEKEA 1779

                         250       260
                  ....*....|....*....|..
gi 52486843  2848 V--DALERTLEQKNKEIEELTK 2867
Cdd:PTZ00121 1780 VieEELDEEDEKRRMEVDKKIK 1801
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2677-2875 1.82e-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: 53.91  E-value: 1.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2677 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREksisHQTVQQLVLEKEQALADL 2756
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL----SKELTELEAEIEELEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2757 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2836
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 52486843   2837 YQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 2875
Cdd:TIGR02168  844 EE---QIEELSED-----IESLAAEIEELEELIEELESE 874
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2701-2876 2.08e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2701 DKYEESRREVVEMRKIVAEYEKtiaqmIEDEQREKSISHQTVQQLVLEKEQALADLnSVEKSLADLFRRYEKMKEVLEGF 2780
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYAE-----LQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAEL 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2781 RKNEEVLKKCAQEYLSRvkkeEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNK 2860
Cdd:COG4717  145 PERLEELEERLEELREL----EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220

                        170
                 ....*....|....*.
gi 52486843 2861 EIEELTKICDELIAKM 2876
Cdd:COG4717  221 ELEELEEELEQLENEL 236
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2607-2865 4.02e-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: 52.76  E-value: 4.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2607 QKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAhppdvsISKTALYSRIGSTEVEKppgLLFQQPDLDSALQVAR 2686
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA------ERYQALLKEKREYEGYE---LLKEKEALERQKEAIE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2687 AEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQRE--KSISHQTVQQLVLEKEQALADLN--SVEKS 2762
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkEKIGELEAEIASLERSIAEKEREleDAEER 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2763 LADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEE---KLDRANAEIAQVRGKAQQEQAAYQA 2839
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkEFAETRDELKDYREKLEKLKREINE 403

                          250       260
                   ....*....|....*....|....*.
gi 52486843   2840 SLRKEqlrvDALERTLEQKNKEIEEL 2865
Cdd:TIGR02169  404 LKREL----DRLQEELQRLSEELADL 425
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2682-2865 8.31e-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: 8.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2682 LQVARAE-VIAKEREVSEWR-----DKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALAD 2755
Cdd:TIGR02168  207 RQAEKAErYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEE-LTAELQELEEKLEELRLEVSELEEEIEE 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2756 LNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqa 2835
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE------ 359

                          170       180       190
                   ....*....|....*....|....*....|
gi 52486843   2836 ayqasLRKEQLRVDALERTLEQKNKEIEEL 2865
Cdd:TIGR02168  360 -----LEELEAELEELESRLEELEEQLETL 384
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2677-2875 9.30e-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: 50.92  E-value: 9.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2677 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALADL 2756
Cdd:COG4942   31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEAQKEELAEL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2757 NSV---------------EKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANA 2821
Cdd:COG4942  110 LRAlyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERA 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 52486843 2822 EIAQVRGKAQQEqaayqasLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 2875
Cdd:COG4942  189 ALEALKAERQKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAE 235
PTZ00121 PTZ00121
MAEBL; Provisional
 2677-2875 1.05e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2677 DLDSALQVARAEVIAKEREV--SEWRDKYEESRREvvEMRKIVAEYEKTIAQMIEdEQREKSISHQTVQQLVLEKEQALA 2754
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKK 1614

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2755 DlnSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEylsrVKKEEQRYqalKVHAEEKLDRANAEiaqvRGKAQQEQ 2834
Cdd:PTZ00121 1615 A--EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEEN---KIKAAEEAKKAEED----KKKAEEAK 1681

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 52486843  2835 AAYQASLRKEQlrvdALERTLEQKNKeIEELTKICDELIAK 2875
Cdd:PTZ00121 1682 KAEEDEKKAAE----ALKKEAEEAKK-AEELKKKEAEEKKK 1717
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2678-2874 1.16e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2678 LDSALQVARAE------VIAKEREVSEWRDKYE-----ESRREVVEMRKIVA---EYEKTIAQMIEDEQREKSISHQTVQ 2743
Cdd:PRK03918  471 IEEKERKLRKElrelekVLKKESELIKLKELAEqlkelEEKLKKYNLEELEKkaeEYEKLKEKLIKLKGEIKSLKKELEK 550

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2744 QLVLEKEQALAD--LNSVEKSLADLFRRYEKmkevlEGFRKNEEV------LKKCAQEYL------SRVKKEEQRYQALK 2809
Cdd:PRK03918  551 LEELKKKLAELEkkLDELEEELAELLKELEE-----LGFESVEELeerlkeLEPFYNEYLelkdaeKELEREEKELKKLE 625

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52486843  2810 ---VHAEEKLDRANAEIAQVRGK----AQQEQAAYQASLRKEQLRvdaLERTLEQKNKEIEELTKICDELIA 2874
Cdd:PRK03918  626 eelDKAFEELAETEKRLEELRKEleelEKKYSEEEYEELREEYLE---LSRELAGLRAELEELEKRREEIKK 694
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2684-2874 1.57e-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: 50.84  E-value: 1.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2684 VARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIED-----EQREKSISHQTVQQ---------LVLEK 2749
Cdd:TIGR02169  153 VERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerlrREREKAERYQALLKekreyegyeLLKEK 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2750 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKE-EQRYQALKvhaeEKLDRANAEIAQVRG 2828
Cdd:TIGR02169  233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVK----EKIGELEAEIASLER 308

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 52486843   2829 KAQQEQAAYQAS---LRKEQLRVDALERTLEQKNKEIEELTKICDELIA 2874
Cdd:TIGR02169  309 SIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
2682-2875 2.30e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 49.14  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2682 LQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMiEDEQreksishQTvQQLVLEKEQALadlnsVEK 2761
Cdd:COG1340   76 LKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL-EWRQ-------QT-EVLSPEEEKEL-----VEK 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2762 sLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEylsRVKKEEQRyQALKVHAEEkLDRANAEIAQVRGKAQqeqaayqaSL 2841
Cdd:COG1340  142 -IKELEKELEKAKKALEKNEKLKELRAELKEL---RKEAEEIH-KKIKELAEE-AQELHEEMIELYKEAD--------EL 207

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 52486843 2842 RKE-----------QLRVDALERTLEQKNKEIEELTKICDELIAK 2875
Cdd:COG1340  208 RKEadelhkeiveaQEKADELHEEIIELQKELRELRKELKKLRKK 252
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2606-2858 2.68e-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: 2.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2606 AQKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAhppdvsisktalysrigSTEVEKppglLFQQPDLDS---AL 2682
Cdd:TIGR02168  283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEEL-----------------EAQLEE----LESKLDELAeelAE 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2683 QVARAEVIAKEREvsEWRDKYEESRREVVEMRKIVAEYEKTIaqmieDEQREKsishqtVQQLVLEKEQALADLNSVEKS 2762
Cdd:TIGR02168  342 LEEKLEELKEELE--SLEAELEELEAELEELESRLEELEEQL-----ETLRSK------VAQLELQIASLNNEIERLEAR 408

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2763 LADLFRRYEKMKEVLEGFRKN-EEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRgkaqQEQAAYQASL 2841
Cdd:TIGR02168  409 LERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE----QALDAAEREL 484

                          250
                   ....*....|....*..
gi 52486843   2842 RKEQLRVDALERTLEQK 2858
Cdd:TIGR02168  485 AQLQARLDSLERLQENL 501
PTZ00121 PTZ00121
MAEBL; Provisional
 2691-2875 2.88e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2691 AKEREVSEWRDKYEESRREVVEMRKIVAEYEKTiaqmiEDEQREKSISHQTVQQLVLEKEQALAD--LNSVEKSLADLFR 2768
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK-----ADEAKKAAEAKKKADEAKKAEEAKKADeaKKAEEAKKADEAK 1540

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2769 RYEKMKEVLEgFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRK-EQLR 2847
Cdd:PTZ00121 1541 KAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaEEAK 1619

                         170       180
                  ....*....|....*....|....*....
gi 52486843  2848 VDALE-RTLEQKNKEIEELTKICDELIAK 2875
Cdd:PTZ00121 1620 IKAEElKKAEEEKKKVEQLKKKEAEEKKK 1648
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2667-2847 4.21e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 4.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2667 KPPGLLFQQPDLDSALQVARAEV---IAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIaQMIEDEQREKSISHQTVQ 2743
Cdd:COG4717   65 KPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAE 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2744 -QLVLEK-EQALADLNSVEKSLADLFRRYEKMKEVLEgfrkneEVLKKCAQEYLSRVKKEEQRYQAL---KVHAEEKLDR 2818
Cdd:COG4717  144 lPERLEElEERLEELRELEEELEELEAELAELQEELE------ELLEQLSLATEEELQDLAEELEELqqrLAELEEELEE 217

                        170       180
                 ....*....|....*....|....*....
gi 52486843 2819 ANAEIAQVRGKAQQEQAAYQASLRKEQLR 2847
Cdd:COG4717  218 AQEELEELEEELEQLENELEAAALEERLK 246
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2692-2867 4.60e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 4.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2692 KEREVSEwrdkYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSIShqtvqqlvLEKEQALADLNSVEKSLADL---FR 2768
Cdd:PRK03918  271 LKKEIEE----LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE--------KRLSRLEEEINGIEERIKELeekEE 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2769 RYEKMKEVLEGFRKNEEVLKKCAQEY---------LSRVKKEEQRYQALKVHAE-EKLDRANAEIaqvrgkaqqeqaayQ 2838
Cdd:PRK03918  339 RLEELKKKLKELEKRLEELEERHELYeeakakkeeLERLKKRLTGLTPEKLEKElEELEKAKEEI--------------E 404

                         170       180
                  ....*....|....*....|....*....
gi 52486843  2839 ASLRKEQLRVDALERTLEQKNKEIEELTK 2867
Cdd:PRK03918  405 EEISKITARIGELKKEIKELKKAIEELKK 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2607-2875 5.44e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 5.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2607 QKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAhppdvsisKTALYSRigSTEVEkppgllfqqpDLDSALQVAR 2686
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEEL--------RLELEEL--ELELE----------EAQAEEYELL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2687 AEVIAKEREVSEWRdkyEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSIShQTVQQLVLEKEQALADLNSVEKSLADL 2766
Cdd:COG1196  295 AELARLEQDIARLE---ERRRELEERLEELEEELAELEEELEELEEELEELE-EELEEAEEELEEAEAELAEAEEALLEA 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2767 FRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRG--KAQQEQAAYQASLRKE 2844
Cdd:COG1196  371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEleEEEEEEEEALEEAAEE 450

                        250       260       270
                 ....*....|....*....|....*....|.
gi 52486843 2845 QLRVDALERTLEQKNKEIEELTKICDELIAK 2875
Cdd:COG1196  451 EAELEEEEEALLELLAELLEEAALLEAALAE 481
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2686-2872 5.93e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 5.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2686 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAE------YEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSV 2759
Cdd:PRK03918  458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKL 537

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2760 EKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKE------------EQRYQALKVHAEEKLDRANAEiaqvr 2827
Cdd:PRK03918  538 KGEIKSLKKELEKLEELKKKLAELEKKLDE-LEEELAELLKEleelgfesveelEERLKELEPFYNEYLELKDAE----- 611

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 52486843  2828 gkaqQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDEL 2872
Cdd:PRK03918  612 ----KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2692-2872 1.20e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.75  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2692 KEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYE 2771
Cdd:PRK03918  336 KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2772 KMKEVLEGFRKNEEVLKK-------CAQEY--------LSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2836
Cdd:PRK03918  416 ELKKEIKELKKAIEELKKakgkcpvCGRELteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL 495

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 52486843  2837 YQASLRKEQLRvdALERTL--------EQKNKEIEELTKICDEL 2872
Cdd:PRK03918  496 IKLKELAEQLK--ELEEKLkkynleelEKKAEEYEKLKEKLIKL 537
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2685-2867 1.24e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2685 ARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVEK--- 2761
Cdd:TIGR02168  668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQlee 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2762 SLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHA---EEKLDRANAEIAQVRGKAQQEQAAYQ 2838
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTLLNEEAANLRERLE 827

                          170       180       190
                   ....*....|....*....|....*....|..
gi 52486843   2839 ASLRK---EQLRVDALERTLEQKNKEIEELTK 2867
Cdd:TIGR02168  828 SLERRiaaTERRLEDLEEQIEELSEDIESLAA 859
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2609-2827 1.95e-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: 47.37  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2609 LQEELEFAVMRIEALKlaRQIALASRSRQDTKREAAHppdvsisktaLYSRIGSTEVEKPpgllfqqpDLDSALQVARAE 2688
Cdd:TIGR02169  292 VKEKIGELEAEIASLE--RSIAEKERELEDAEERLAK----------LEAEIDKLLAEIE--------ELEREIEEERKR 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2689 VIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM---IEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLAD 2765
Cdd:TIGR02169  352 RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYrekLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG 431

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52486843   2766 LFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKvhaeEKLDRANAEIAQVR 2827
Cdd:TIGR02169  432 IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK----EEYDRVEKELSKLQ 489
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
2000-2111 2.19e-04

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 46.27  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2000 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 2072
Cdd:PRK13335   45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 52486843  2073 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 2111
Cdd:PRK13335  125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2608-2878 2.41e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2608 KLQEELEFAVMRIE--ALKLARQIALASRSRQDTKREAAHPPDvsisktalysrigstEVEKppgllfqqpDLDSaLQVA 2685
Cdd:PRK03918  345 KKLKELEKRLEELEerHELYEEAKAKKEELERLKKRLTGLTPE---------------KLEK---------ELEE-LEKA 399

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2686 RAEViakEREVSEWRDKYEESRREVVEMRKIVAEYEK------TIAQMIEDEQRE----------KSIShQTVQQLVLEK 2749
Cdd:PRK03918  400 KEEI---EEEISKITARIGELKKEIKELKKAIEELKKakgkcpVCGRELTEEHRKelleeytaelKRIE-KELKEIEEKE 475

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2750 EQALADLNSVEKSLADLfRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEeqrYQALKvhaeEKLDRANAEIaqvrgk 2829
Cdd:PRK03918  476 RKLRKELRELEKVLKKE-SELIKLKELAEQLKELEEKLKKYNLEELEKKAEE---YEKLK----EKLIKLKGEI------ 541

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 52486843  2830 aqqeqaayqASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGK 2878
Cdd:PRK03918  542 ---------KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2704-2867 3.11e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 3.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2704 EESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKN 2783
Cdd:COG4372   31 EQLRKALFELDKLQEELEQLREE-LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2784 EEVLkkcaQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQvrgkaqqeqaayqaslRKEQLrvDALERTLEQKNKEIE 2863
Cdd:COG4372  110 AEEL----QEELEELQKERQDLEQQRKQLEAQIAELQSEIAE----------------REEEL--KELEEQLESLQEELA 167


                 ....
gi 52486843 2864 ELTK 2867
Cdd:COG4372  168 ALEQ 171
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2682-2823 3.74e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2682 LQVARAEVIAKEREVSEWRDKYEESRREVVEMRKI--VAEYEKtiaqmIEDEQREKSISHQTVQQlvlEKEQALADLNSV 2759
Cdd:PRK03918  621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEE-----LREEYLELSRELAGLRA---ELEELEKRREEI 692

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52486843  2760 EKSLADLFRRYEKMKEVlegfRKNEEVLKKcAQEYLSRVKKEEQRYQAL-KVHAEEKLDRANAEI 2823
Cdd:PRK03918  693 KKTLEKLKEELEEREKA----KKELEKLEK-ALERVEELREKVKKYKALlKERALSKVGEIASEI 752
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2681-2865 4.00e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 4.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2681 ALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKI----------------VAEYEKTIAQmIEDEQREKSISHQTVQQ 2744
Cdd:COG4913  611 KLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAE-LEAELERLDASSDDLAA 689

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2745 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIA 2824
Cdd:COG4913  690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD-RLEAAEDLARLELRALLEERFAAALGDAVERELR 768

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 52486843 2825 QvrgkaqqeqaayqaSLRKeqlRVDALERTLEQKNKEIEEL 2865
Cdd:COG4913  769 E--------------NLEE---RIDALRARLNRAEEELERA 792
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
2686-2878 4.81e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.90  E-value: 4.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2686 RAEVIAkerEVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIE------DEQREKSISHQTVQQLVLEKEQALADLNSV 2759
Cdd:COG1340   31 RDELNE---ELKELAEKRDELNAQVKELREEAQELREKRDELNEkvkelkEERDELNEKLNELREELDELRKELAELNKA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2760 EKSLADLFRRYEKM--------------KEVLEGFRKNEEVLK--KCAQEYLSRVKKEEQRYQALKVHAE---------- 2813
Cdd:COG1340  108 GGSIDKLRKEIERLewrqqtevlspeeeKELVEKIKELEKELEkaKKALEKNEKLKELRAELKELRKEAEeihkkikela 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52486843 2814 EKLDRANAEIAQVRGKaqqeqaayQASLRKEqlrVDALERTLEQKNKEIEELTKICDELIAKMGK 2878
Cdd:COG1340  188 EEAQELHEEMIELYKE--------ADELRKE---ADELHKEIVEAQEKADELHEEIIELQKELRE 241
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2672-2864 1.98e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2672 LFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEyektIAQMIEDEQREKSISHQTVQQLVLEKEQ 2751
Cdd:COG4372   37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE----LNEQLQAAQAELAQAQEELESLQEEAEE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2752 ALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQAL-KVHAEEKLDRANAEIAQV---- 2826
Cdd:COG4372  113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALeQELQALSEAEAEQALDELlkea 192

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 52486843 2827 -RGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEE 2864
Cdd:COG4372  193 nRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 2591-2873 2.83e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 43.29  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2591 GYlepDLAEKNPPVFAQKLQEELEFAVMRIEALKLARqialASRSRQDTKREaahppdvsisKTALYSRIgSTEVEKPPG 2670
Cdd:PRK04778  246 GY---HLDHLDIEKEIQDLKEQIDENLALLEELDLDE----AEEKNEEIQER----------IDQLYDIL-EREVKARKY 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2671 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQR--EKSISHQTVQqlvle 2748
Cdd:PRK04778  308 VEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERiaEQEIAYSELQ----- 382

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2749 keqalADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLS-------RVKKEE-----QRYQALKVHAEEKL 2816
Cdd:PRK04778  383 -----EELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNklheikrYLEKSNlpglpEDYLEMFFEVSDEI 457

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 52486843  2817 DRANAEIAQVRgkaqqeqaayqaslrkeqLRVDALERTLEQKNKEIEELTKICDELI 2873
Cdd:PRK04778  458 EALAEELEEKP------------------INMEAVNRLLEEATEDVETLEEETEELV 496
PTZ00121 PTZ00121
MAEBL; Provisional
 2677-2875 3.06e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2677 DLDSALQVARAEVIAKEREV---------SEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVL 2747
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKkkadeakkkAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2748 EKEQALAD--LNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEE--KLDRANAEI 2823
Cdd:PTZ00121 1362 AEEKAEAAekKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEEkkKADEAKKKA 1440

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 52486843  2824 AQVRgKAQQEQAAYQASLRKEQLRVDALE-RTLEQKNKEIEELTKiCDELIAK 2875
Cdd:PTZ00121 1441 EEAK-KADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKK-ADEAKKK 1491
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 2695-2867 3.19e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 3.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2695 EVSEWRDKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMK 2774
Cdd:TIGR04523  315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQ-LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2775 EVLEG-FRKNEEV-------LKKCAQEYLSrVKKEEQRYQALKVHAEEKLDRANAEIA----------QVRGKAQQEQAA 2836
Cdd:TIGR04523  394 NDLESkIQNQEKLnqqkdeqIKKLQQEKEL-LEKEIERLKETIIKNNSEIKDLTNQDSvkeliiknldNTRESLETQLKV 472

                          170       180       190
                   ....*....|....*....|....*....|.
gi 52486843   2837 YQASLRKEQLRVDALERTLEQKNKEIEELTK 2867
Cdd:TIGR04523  473 LSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 2611-2864 3.35e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.19  E-value: 3.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2611 EELEFAVMRIEALKLARQIalaSRSRQDTKREAAHPPDVSiSKTALYSRIGSTEVEKPPGL-LFQQPDLDSALQVARAEV 2689
Cdd:pfam17380  294 EKMEQERLRQEKEEKAREV---ERRRKLEEAEKARQAEMD-RQAAIYAEQERMAMERERELeRIRQEERKRELERIRQEE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2690 IAKEREVSEWRDKYEESRREVVEmrKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQaladlnsvEKSLADLFRR 2769
Cdd:pfam17380  370 IAMEISRMRELERLQMERQQKNE--RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ--------EEARQREVRR 439

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2770 YEKMKEvLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKlDRANAEiAQVRGKAQQEQAAYQASLRKEQLRVD 2849
Cdd:pfam17380  440 LEEERA-REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKR-DRKRAE-EQRRKILEKELEERKQAMIEEERKRK 516

                          250
                   ....*....|....*
gi 52486843   2850 ALERTLEQKNKEIEE 2864
Cdd:pfam17380  517 LLEKEMEERQKAIYE 531
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 2683-2864 4.94e-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: 41.83  E-value: 4.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2683 QVARAEVIAKEREVSEWRDK-YEESRREvvEMRkiVAEYEKTIAQ---MIEDEQREKSISHQTVQQLVL----------- 2747
Cdd:pfam13868  126 RQLREEIDEFNEEQAEWKELeKEEEREE--DER--ILEYLKEKAEreeEREAEREEIEEEKEREIARLRaqqekaqdeka 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2748 EKEQALADLNSVE-------KSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYlsRVKKEEQRYQALKVHAE-EKLDRA 2819
Cdd:pfam13868  202 ERDELRAKLYQEEqerkerqKEREEAEKKARQRQELQQAREEQIELKERRLAEE--AEREEEEFERMLRKQAEdEEIEQE 279

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 52486843   2820 NAEiaQVRGKAQQEQAAYQASLR-KEQLRVDALERTLEQKNKEIEE 2864
Cdd:pfam13868  280 EAE--KRRMKRLEHRRELEKQIEeREEQRAAEREEELEEGERLREE 323
PTZ00121 PTZ00121
MAEBL; Provisional
 2681-2872 5.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2681 ALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIE-DEQREKSISHQTVQQLVLEKEQALADLNSV 2759
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAAAAKKKADEA 1423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2760 EKSlADLFRRYEKMKEVLEGFRKNEEVLKKCAQ----EYLSRVKKEEQRYQALKVHAEE--KLDRANAEIAQVRGKAQQE 2833
Cdd:PTZ00121 1424 KKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEakkaEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEA 1502

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 52486843  2834 QAAYQASLRKEQLRvDALERTLEQKNKEIEELTKiCDEL 2872
Cdd:PTZ00121 1503 KKAAEAKKKADEAK-KAEEAKKADEAKKAEEAKK-ADEA 1539
PRK12704 PRK12704
phosphodiesterase; Provisional
 2685-2825 5.37e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2685 ARAEVIAKEREVsEWRDKYEESR----REVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVE 2760
Cdd:PRK12704   49 KEAEAIKKEALL-EAKEEIHKLRnefeKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52486843  2761 KSLADLFRRYEKMKEVLE---GFRKNE-------EVLKKCAQEYLSRVKKEEQRyqalkvhAEEKLDR-ANAEIAQ 2825
Cdd:PRK12704  128 KKEEELEELIEEQLQELErisGLTAEEakeilleKVEEEARHEAAVLIKEIEEE-------AKEEADKkAKEILAQ 196
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 2716-2865 5.76e-03

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 40.66  E-value: 5.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2716 IVAEYEKTIAQMiedeqrEKSISHQTVQQLVL------EKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKK 2789
Cdd:pfam13851    2 LMKNHEKAFNEI------KNYYNDITRNNLELikslkeEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2790 CAQEYL----------SRVKKEEQRYQALKVHAEEKL--------------DRANAEIAQVRGKaqqeqaayqaSLRKEQ 2845
Cdd:pfam13851   76 QLENYEkdkqslknlkARLKVLEKELKDLKWEHEVLEqrfekvererdelyDKFEAAIQDVQQK----------TGLKNL 145

                          170       180
                   ....*....|....*....|...
gi 52486843   2846 L---RVDALERTLEQKNKEIEEL 2865
Cdd:pfam13851  146 LlekKLQALGETLEKKEAQLNEV 168
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 2697-2875 6.01e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 6.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2697 SEWRDKYEESRREVVEMRKIVAEyEKTIAQMIEDEQREKSISHQTVQQLVLEKEQaladlnsVEKSLADLFRRYEKMKev 2776
Cdd:TIGR04523  482 QNLEQKQKELKSKEKELKKLNEE-KKELEEKVKDLTKKISSLKEKIEKLESEKKE-------KESKISDLEDELNKDD-- 551

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2777 legFRKNEEVLKKCAQEYLSRVKKEEQRYQALKV---HAEEKLDRANAEIAQVR------GKAQQEQAAYQASLRKEQLR 2847
Cdd:TIGR04523  552 ---FELKKENLEKEIDEKNKEIEELKQTQKSLKKkqeEKQELIDQKEKEKKDLIkeieekEKKISSLEKELEKAKKENEK 628

                          170       180       190
                   ....*....|....*....|....*....|..
gi 52486843   2848 VDALERTLEQK----NKEIEELTKICDELIAK 2875
Cdd:TIGR04523  629 LSSIIKNIKSKknklKQEVKQIKETIKEIRNK 660
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2742-2866 7.78e-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: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2742 VQQLVLEKEQALADLNsvekSLADLFRRYEKMKEVLEGFRKNEEVL---KKCAQEYLS-RVKKEEQRYQALKVH---AEE 2814
Cdd:COG4913  213 VREYMLEEPDTFEAAD----ALVEHFDDLERAHEALEDAREQIELLepiRELAERYAAaRERLAELEYLRAALRlwfAQR 288

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 52486843 2815 KLDRANAEIAQVRgkaqqeqaayqASLRKEQLRVDALERTLEQKNKEIEELT 2866
Cdd:COG4913  289 RLELLEAELEELR-----------AELARLEAELERLEARLDALREELDELE 329
PRK01156 PRK01156
chromosome segregation protein; Provisional
 2686-2864 7.91e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.81  E-value: 7.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2686 RAEVIAKER-EVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLA 2764
Cdd:PRK01156  347 RYDDLNNQIlELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843  2765 DLFRRYEKMKEVLEGFRKNEEVLK---KC-------AQEYLSRVKKEeqrYQALKVHAEEKLDRANAEIAQVRGKAQQEQ 2834
Cdd:PRK01156  427 SLNQRIRALRENLDELSRNMEMLNgqsVCpvcgttlGEEKSNHIINH---YNEKKSRLEEKIREIEIEVKDIDEKIVDLK 503

                         170       180       190
                  ....*....|....*....|....*....|
gi 52486843  2835 AAYQASLRKEQLRVDALERTLEQKNKEIEE 2864
Cdd:PRK01156  504 KRKEYLESEEINKSINEYNKIESARADLED 533
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 2686-2871 8.32e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.88  E-value: 8.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2686 RAEVIAKEREVsewrdkyEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTV--QQLVLEKEQALADLNSVEKSL 2763
Cdd:pfam02463  185 LAELIIDLEEL-------KLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLneERIDLLQELLRDEQEEIESSK 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843   2764 ADLFRRYEKMKEVLEGFRKNEEVLK-----------KCAQEYLSRVKKEEQRYQALK--VHAEEKLDRANAEIAQVRGKA 2830
Cdd:pfam02463  258 QEIEKEEEKLAQVLKENKEEEKEKKlqeeelkllakEEEELKSELLKLERRKVDDEEklKESEKEKKKAEKELKKEKEEI 337

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 52486843   2831 QQEQAAYQASLRKEQL----RVDALERTLEQKNKEIEELTKICDE 2871
Cdd:pfam02463  338 EELEKELKELEIKREAeeeeEEELEKLQEKLEQLEEELLAKKKLE 382
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 2677-2876 8.73e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 8.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2677 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEyektiaqmIEDEQREKSISHQTVQQLVLEKEQALA-- 2754
Cdd:COG1579   14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED--------LEKEIKRLELEIEEVEARIKKYEEQLGnv 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2755 ----DLNSVEKSLADLfrryEKMKEVLEgfrknEEVLkkcaqeylsrvkkeeqryqalkvHAEEKLDRANAEIAQVRGKA 2830
Cdd:COG1579   86 rnnkEYEALQKEIESL----KRRISDLE-----DEIL-----------------------ELMERIEELEEELAELEAEL 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 52486843 2831 QQeqaayqaslRKEQLR--VDALERTLEQKNKEIEELTKICDELIAKM 2876
Cdd:COG1579  134 AE---------LEAELEekKAELDEELAELEAELEELEAEREELAAKI 172
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
2678-2872 9.66e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 9.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2678 LDSALQVARAEViakeREVSEW-RDKYEESRREVVEMRKIVAEYEKtiAQMIEDEQREKSISHQTVQQLVLEKEQALADL 2756
Cdd:COG3206  162 LEQNLELRREEA----RKALEFlEEQLPELRKELEEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486843 2757 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVlkkcaQEYLSRVKKEEQRYQALKVHAEEK---LDRANAEIAQVRGKAQQE 2833
Cdd:COG3206  236 AEAEARLAALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQE 310

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 52486843 2834 QAAYQASLRKE----QLRVDALERTLEQKNKEIEELTKICDEL 2872
Cdd:COG3206  311 AQRILASLEAElealQAREASLQAQLAQLEARLAELPELEAEL 353
 
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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