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Conserved domains on  [gi|1039779424|ref|XP_017177889|]
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transforming acidic coiled-coil-containing protein 2 isoform X11 [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 ...
2684-2884 1.74e-105

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: 335.88  E-value: 1.74e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2684 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQA 2763
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2764 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 2843
Cdd:pfam05010   81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1039779424 2844 EQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 2884
Cdd:pfam05010  161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
PRK13335 super family cl31400
superantigen-like protein SSL3; Reviewed;
2053-2164 2.18e-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: 2.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2053 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 2125
Cdd:PRK13335    45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1039779424 2126 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 2164
Cdd:PRK13335   125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
1748-2120 3.53e-04

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 3.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 1748 PPEPDESKDEKLHLVAPEELLSDRK-------SPGPGPATLPSVPEACVPKGFPAEARDLGGVESIPGTDDVIQPAAPVD 1820
Cdd:PHA03307    79 APANESRSTPTWSLSTLAPASPAREgsptppgPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGAS 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 1821 PGHPP--LADSSHHGDAVSSVSTHLTVQSASPSAARASPAPLAPEHTASAPSA-AGPGVEVTPTASPQHLAKNEPRSSDS 1897
Cdd:PHA03307   159 PAAVAsdAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSpISASASSPAPAPGRSAADDAGASSSD 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 1898 EEAFETPESTTPVKAPPAPPPpppevtpepevidPPAPEEPGCISEPPVVVPDGPRSSESVEGSPFRPSHSSSAVFDEDK 1977
Cdd:PHA03307   239 SSSSESSGCGWGPENECPLPR-------------PAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGS 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 1978 PIASSGTYNLDfdsielvdnFQSLEPCSADSKGQECKVSTRrksTESVPPSKStLSRSLSLQaSDFDGASCPGSPEAGTL 2057
Cdd:PHA03307   306 GPAPSSPRASS---------SSSSSRESSSSSTSSSSESSR---GAAVSPGPS-PSRSPSPS-RPPPPADPSSPRKRPRP 371
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779424 2058 TTDACGTGSNSASSTLKRTKKTRPPSLKKKQAT-KKPTETPPVKETQQEPGEESPVPSEEHLAP 2120
Cdd:PHA03307   372 SRAPSSPAASAGRPTRRRARAAVAGRARRRDATgRFPAGRPRPSPLDAGAASGAFYARYPLLTP 435
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
2684-2884 1.74e-105

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: 335.88  E-value: 1.74e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2684 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQA 2763
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2764 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 2843
Cdd:pfam05010   81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1039779424 2844 EQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 2884
Cdd:pfam05010  161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2682-2888 2.31e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.08  E-value: 2.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2682 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKT---IAQM-IEDEQREKSIshQTVQQLV 2757
Cdd:PRK03918   184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEELeKELESLEGSK--RKLEEKI 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2758 LEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA----- 2832
Cdd:PRK03918   262 RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkeerl 340
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779424 2833 ------------EIAQVRGKAQQEQAAYQASLRKEQLR-------VDALERTLEQKNKEIEELTKICDELIAKMG 2888
Cdd:PRK03918   341 eelkkklkelekRLEELEERHELYEEAKAKKEELERLKkrltgltPEKLEKELEELEKAKEEIEEEISKITARIG 415
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2688-2885 8.00e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 8.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2688 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKsishQTVQQLVLEKEQALADL 2767
Cdd:COG1196    250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEEL 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2768 NSVEKSLADLfrrYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2847
Cdd:COG1196    326 AELEEELEEL---EEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1039779424 2848 YQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIA 2885
Cdd:COG1196    402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2688-2886 1.59e-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: 54.29  E-value: 1.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2688 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREksisHQTVQQLVLEKEQALADL 2767
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL----SKELTELEAEIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2768 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2847
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1039779424 2848 YQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 2886
Cdd:TIGR02168  844 EE---QIEELSED-----IESLAAEIEELEELIEELESE 874
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
2053-2164 2.18e-04

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 46.27  E-value: 2.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2053 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 2125
Cdd:PRK13335    45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1039779424 2126 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 2164
Cdd:PRK13335   125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1748-2120 3.53e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 3.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 1748 PPEPDESKDEKLHLVAPEELLSDRK-------SPGPGPATLPSVPEACVPKGFPAEARDLGGVESIPGTDDVIQPAAPVD 1820
Cdd:PHA03307    79 APANESRSTPTWSLSTLAPASPAREgsptppgPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGAS 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 1821 PGHPP--LADSSHHGDAVSSVSTHLTVQSASPSAARASPAPLAPEHTASAPSA-AGPGVEVTPTASPQHLAKNEPRSSDS 1897
Cdd:PHA03307   159 PAAVAsdAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSpISASASSPAPAPGRSAADDAGASSSD 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 1898 EEAFETPESTTPVKAPPAPPPpppevtpepevidPPAPEEPGCISEPPVVVPDGPRSSESVEGSPFRPSHSSSAVFDEDK 1977
Cdd:PHA03307   239 SSSSESSGCGWGPENECPLPR-------------PAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGS 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 1978 PIASSGTYNLDfdsielvdnFQSLEPCSADSKGQECKVSTRrksTESVPPSKStLSRSLSLQaSDFDGASCPGSPEAGTL 2057
Cdd:PHA03307   306 GPAPSSPRASS---------SSSSSRESSSSSTSSSSESSR---GAAVSPGPS-PSRSPSPS-RPPPPADPSSPRKRPRP 371
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779424 2058 TTDACGTGSNSASSTLKRTKKTRPPSLKKKQAT-KKPTETPPVKETQQEPGEESPVPSEEHLAP 2120
Cdd:PHA03307   372 SRAPSSPAASAGRPTRRRARAAVAGRARRRDATgRFPAGRPRPSPLDAGAASGAFYARYPLLTP 435
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
2684-2884 1.74e-105

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: 335.88  E-value: 1.74e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2684 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQA 2763
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2764 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 2843
Cdd:pfam05010   81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1039779424 2844 EQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 2884
Cdd:pfam05010  161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2682-2888 2.31e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.08  E-value: 2.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2682 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKT---IAQM-IEDEQREKSIshQTVQQLV 2757
Cdd:PRK03918   184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEELeKELESLEGSK--RKLEEKI 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2758 LEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA----- 2832
Cdd:PRK03918   262 RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkeerl 340
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779424 2833 ------------EIAQVRGKAQQEQAAYQASLRKEQLR-------VDALERTLEQKNKEIEELTKICDELIAKMG 2888
Cdd:PRK03918   341 eelkkklkelekRLEELEERHELYEEAKAKKEELERLKkrltgltPEKLEKELEELEKAKEEIEEEISKITARIG 415
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2688-2885 8.00e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 8.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2688 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKsishQTVQQLVLEKEQALADL 2767
Cdd:COG1196    250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEEL 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2768 NSVEKSLADLfrrYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2847
Cdd:COG1196    326 AELEEELEEL---EEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1039779424 2848 YQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIA 2885
Cdd:COG1196    402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2712-2887 1.48e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.00  E-value: 1.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2712 DKYEESRREVVEMRKIVAEYEKtiaqmIEDEQREKSISHQTVQQLVLEKEQALADLnSVEKSLADLFRRYEKMKEVLEGF 2791
Cdd:COG4717     71 KELKELEEELKEAEEKEEEYAE-----LQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAEL 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2792 RKNEEVLKKCAQEYLSRvkkeEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNK 2871
Cdd:COG4717    145 PERLEELEERLEELREL----EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
                          170
                   ....*....|....*.
gi 1039779424 2872 EIEELTKICDELIAKM 2887
Cdd:COG4717    221 ELEELEEELEQLENEL 236
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2688-2886 1.59e-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: 54.29  E-value: 1.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2688 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREksisHQTVQQLVLEKEQALADL 2767
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL----SKELTELEAEIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2768 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2847
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1039779424 2848 YQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 2886
Cdd:TIGR02168  844 EE---QIEELSED-----IESLAAEIEELEELIEELESE 874
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2645-2878 4.52e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 4.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2645 VFAQKLQREAAhppdvsisktALYSRIGSteveKPPGLLFQQPDLDSALQVARAEV---IAKEREVSEWRDKYEESRREV 2721
Cdd:COG4717     46 MLLERLEKEAD----------ELFKPQGR----KPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAEL 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2722 VEMRKIVAEYEKTIAqmiedeqreksishqtVQQLVLEKEQAladlnsvEKSLADLFRRYEKMKEVLEGFRKNEEVLKKC 2801
Cdd:COG4717    112 EELREELEKLEKLLQ----------------LLPLYQELEAL-------EAELAELPERLEELEERLEELRELEEELEEL 168
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779424 2802 AQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEIEELTK 2878
Cdd:COG4717    169 EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-----------LAELEEELEEAQEELEELEEELEQLEN 234
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2693-2876 6.43e-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: 51.98  E-value: 6.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2693 LQVARAE-VIAKEREVSEWR-----DKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALAD 2766
Cdd:TIGR02168  207 RQAEKAErYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEE-LTAELQELEEKLEELRLEVSELEEEIEE 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2767 LNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqa 2846
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE------ 359
                          170       180       190
                   ....*....|....*....|....*....|
gi 1039779424 2847 ayqasLRKEQLRVDALERTLEQKNKEIEEL 2876
Cdd:TIGR02168  360 -----LEELEAELEELESRLEELEEQLETL 384
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2648-2884 6.92e-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: 51.99  E-value: 6.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2648 QKLQREAAHppdvSISKTALYSRIGSTEVEKppgLLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKI 2727
Cdd:TIGR02169  201 ERLRREREK----AERYQALLKEKREYEGYE---LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2728 VAEYEKTIAQMIEDEQRE--KSISHQTVQQLVLEKEQALADLN--SVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQ 2803
Cdd:TIGR02169  274 LEELNKKIKDLGEEEQLRvkEKIGELEAEIASLERSIAEKEREleDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2804 EYLSRVKKEEQRYQALKVHAEEkLDRANAEiaqvrgkaqqeqaayqasLRKEQlrvDALERTLEQKNKEIEELTKICDEL 2883
Cdd:TIGR02169  354 KLTEEYAELKEELEDLRAELEE-VDKEFAE------------------TRDEL---KDYREKLEKLKREINELKRELDRL 411

                   .
gi 1039779424 2884 I 2884
Cdd:TIGR02169  412 Q 412
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2688-2886 7.51e-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: 7.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2688 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALAD- 2766
Cdd:COG4942     31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEAQKEELAEl 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2767 ----------------LNSveKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRA 2830
Cdd:COG4942    110 lralyrlgrqpplallLSP--EDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEE 186
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779424 2831 NAEIAQVRGKAQQEqaayqasLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 2886
Cdd:COG4942    187 RAALEALKAERQKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAE 235
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2689-2885 7.76e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 7.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2689 LDSALQVARAE------VIAKEREVSEWRDKYE-----ESRREVVEMRKIVA---EYEKTIAQMIEDEQREKSISHQTVQ 2754
Cdd:PRK03918   471 IEEKERKLRKElrelekVLKKESELIKLKELAEqlkelEEKLKKYNLEELEKkaeEYEKLKEKLIKLKGEIKSLKKELEK 550
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2755 QLVLEKEQALAD--LNSVEKSLADLFRRYEKmkevlEGFRKNEEV------LKKCAQEYL------SRVKKEEQRYQALK 2820
Cdd:PRK03918   551 LEELKKKLAELEkkLDELEEELAELLKELEE-----LGFESVEELeerlkeLEPFYNEYLelkdaeKELEREEKELKKLE 625
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779424 2821 ---VHAEEKLDRANAEIAQVRGK----AQQEQAAYQASLRKEQLRvdaLERTLEQKNKEIEELTKICDELIA 2885
Cdd:PRK03918   626 eelDKAFEELAETEKRLEELRKEleelEKKYSEEEYEELREEYLE---LSRELAGLRAELEELEKRREEIKK 694
PTZ00121 PTZ00121
MAEBL; Provisional
2688-2886 1.03e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2688 DLDSALQVARAEVIAKEREV--SEWRDKYEESRREvvEMRKIVAEYEKTIAQMIEdEQREKSISHQTVQQLVLEKEQALA 2765
Cdd:PTZ00121  1538 EAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKK 1614
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2766 DlnSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEylsrVKKEEQRYqalKVHAEEKLDRANAEiaqvRGKAQQEQ 2845
Cdd:PTZ00121  1615 A--EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEEN---KIKAAEEAKKAEED----KKKAEEAK 1681
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1039779424 2846 AAYQASLRKEQlrvdALERTLEQKNKeIEELTKICDELIAK 2886
Cdd:PTZ00121  1682 KAEEDEKKAAE----ALKKEAEEAKK-AEELKKKEAEEKKK 1717
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
2693-2886 1.17e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 49.91  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2693 LQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMiEDEQreksishQTvQQLVLEKEQALadlnsVEK 2772
Cdd:COG1340     76 LKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL-EWRQ-------QT-EVLSPEEEKEL-----VEK 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2773 sLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEylsRVKKEEQRyQALKVHAEEkLDRANAEIAQVRGKAQqeqaayqaSL 2852
Cdd:COG1340    142 -IKELEKELEKAKKALEKNEKLKELRAELKEL---RKEAEEIH-KKIKELAEE-AQELHEEMIELYKEAD--------EL 207
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1039779424 2853 RKE-----------QLRVDALERTLEQKNKEIEELTKICDELIAK 2886
Cdd:COG1340    208 RKEadelhkeiveaQEKADELHEEIIELQKELRELRKELKKLRKK 252
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2695-2885 1.26e-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: 51.22  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2695 VARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIED-----EQREKSISHQTVQQ---------LVLEK 2760
Cdd:TIGR02169  153 VERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerlrREREKAERYQALLKekreyegyeLLKEK 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2761 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKE-EQRYQALKvhaeEKLDRANAEIAQVRG 2839
Cdd:TIGR02169  233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVK----EKIGELEAEIASLER 308
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1039779424 2840 KAQQEQAAYQAS---LRKEQLRVDALERTLEQKNKEIEELTKICDELIA 2885
Cdd:TIGR02169  309 SIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
PTZ00121 PTZ00121
MAEBL; Provisional
2702-2886 2.94e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 2.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2702 AKEREVSEWRDKYEESRREVVEMRKIVAEYEKTiaqmiEDEQREKSISHQTVQQLVLEKEQALAD--LNSVEKSLADLFR 2779
Cdd:PTZ00121  1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK-----ADEAKKAAEAKKKADEAKKAEEAKKADeaKKAEEAKKADEAK 1540
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2780 RYEKMKEVLEgFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRK-EQLR 2858
Cdd:PTZ00121  1541 KAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaEEAK 1619
                          170       180
                   ....*....|....*....|....*....
gi 1039779424 2859 VDALE-RTLEQKNKEIEELTKICDELIAK 2886
Cdd:PTZ00121  1620 IKAEElKKAEEEKKKVEQLKKKEAEEKKK 1648
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2685-2869 3.41e-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: 3.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2685 QQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM--IEDEQREKSISHQT-VQQLVLEKE 2761
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesRLEELEEQLETLRSkVAQLELQIA 396
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2762 QALADLNSVEKSLADLFRRYEKMKEVLEGFRKN-EEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRgk 2840
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE-- 474
                          170       180
                   ....*....|....*....|....*....
gi 1039779424 2841 aqQEQAAYQASLRKEQLRVDALERTLEQK 2869
Cdd:TIGR02168  475 --QALDAAERELAQLQARLDSLERLQENL 501
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2703-2878 3.47e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 3.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2703 KEREVSEwrdkYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSIShqtvqqlvLEKEQALADLNSVEKSLADL---FR 2779
Cdd:PRK03918   271 LKKEIEE----LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE--------KRLSRLEEEINGIEERIKELeekEE 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2780 RYEKMKEVLEGFRKNEEVLKKCAQEY---------LSRVKKEEQRYQALKVHAE-EKLDRANAEIaqvrgkaqqeqaayQ 2849
Cdd:PRK03918   339 RLEELKKKLKELEKRLEELEERHELYeeakakkeeLERLKKRLTGLTPEKLEKElEELEKAKEEI--------------E 404
                          170       180
                   ....*....|....*....|....*....
gi 1039779424 2850 ASLRKEQLRVDALERTLEQKNKEIEELTK 2878
Cdd:PRK03918   405 EEISKITARIGELKKEIKELKKAIEELKK 433
PTZ00121 PTZ00121
MAEBL; Provisional
2690-2878 3.56e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 3.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2690 DSALQVARAEVI--AKEREVSEWRDKYEESRREVVE-MRKivAEYEKTIAQMIEDEQREKsishQTVQQLVLEKEQalad 2766
Cdd:PTZ00121  1575 DKNMALRKAEEAkkAEEARIEEVMKLYEEEKKMKAEeAKK--AEEAKIKAEELKKAEEEK----KKVEQLKKKEAE---- 1644
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2767 lnsvEKSLADLFRRYEKMKEV-LEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKldranAEIAQVRgKAQQEQ 2845
Cdd:PTZ00121  1645 ----EKKKAEELKKAEEENKIkAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-----KKAEELK-KKEAEE 1714
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1039779424 2846 AAYQASLRKEQ----LRVDALERTLEQKNKEIEELTK 2878
Cdd:PTZ00121  1715 KKKAEELKKAEeenkIKAEEAKKEAEEDKKKAEEAKK 1751
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2697-2883 4.86e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 4.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2697 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAE------YEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSV 2770
Cdd:PRK03918   458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKL 537
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2771 EKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKE------------EQRYQALKVHAEEKLDRANAEiaqvr 2838
Cdd:PRK03918   538 KGEIKSLKKELEKLEELKKKLAELEKKLDE-LEEELAELLKEleelgfesveelEERLKELEPFYNEYLELKDAE----- 611
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1039779424 2839 gkaqQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDEL 2883
Cdd:PRK03918   612 ----KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
PTZ00121 PTZ00121
MAEBL; Provisional
2683-2878 6.36e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 6.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2683 LFQQPDLDSALQVARAEviaKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQ 2762
Cdd:PTZ00121  1600 LYEEEKKMKAEEAKKAE---EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2763 A--LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYlsRVKKEEQRYQALKVHAEEKLDRANAEIAQVR-- 2838
Cdd:PTZ00121  1677 AeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL--KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDee 1754
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1039779424 2839 -----GKAQQEQAAYQASLRKEQLRV--DALERTLEQKNKEIEELTK 2878
Cdd:PTZ00121  1755 ekkkiAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIK 1801
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2703-2883 9.64e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 9.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2703 KEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYE 2782
Cdd:PRK03918   336 KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2783 KMKEVLEGFRKNEEVLKK-------CAQEY--------LSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2847
Cdd:PRK03918   416 ELKKEIKELKKAIEELKKakgkcpvCGRELteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL 495
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1039779424 2848 YQASLRKEQLRvdALERTL--------EQKNKEIEELTKICDEL 2883
Cdd:PRK03918   496 IKLKELAEQLK--ELEEKLkkynleelEKKAEEYEKLKEKLIKL 537
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2696-2878 9.69e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 9.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2696 ARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVEK--- 2772
Cdd:TIGR02168  668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQlee 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2773 SLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHA---EEKLDRANAEIAQVRGKAQQEQAAYQ 2849
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTLLNEEAANLRERLE 827
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1039779424 2850 ASLRK---EQLRVDALERTLEQKNKEIEELTK 2878
Cdd:TIGR02168  828 SLERRiaaTERRLEDLEEQIEELSEDIESLAA 859
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2715-2878 1.54e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2715 EESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKN 2794
Cdd:COG4372     31 EQLRKALFELDKLQEELEQLREE-LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2795 EEVLkkcaQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQvrgkaqqeqaayqaslRKEQLrvDALERTLEQKNKEIE 2874
Cdd:COG4372    110 AEEL----QEELEELQKERQDLEQQRKQLEAQIAELQSEIAE----------------REEEL--KELEEQLESLQEELA 167

                   ....
gi 1039779424 2875 ELTK 2878
Cdd:COG4372    168 ALEQ 171
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2704-2889 1.85e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2704 EREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM-------------IEDEQRE----------KSIShQTVQQLVLEK 2760
Cdd:PRK03918   397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgreLTEEHRKelleeytaelKRIE-KELKEIEEKE 475
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2761 EQALADLNSVEKSLADLfRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEeqrYQALKvhaeEKLDRANAEIaqvrgk 2840
Cdd:PRK03918   476 RKLRKELRELEKVLKKE-SELIKLKELAEQLKELEEKLKKYNLEELEKKAEE---YEKLK----EKLIKLKGEI------ 541
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1039779424 2841 aqqeqaayqASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGK 2889
Cdd:PRK03918   542 ---------KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
2053-2164 2.18e-04

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 46.27  E-value: 2.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2053 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 2125
Cdd:PRK13335    45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1039779424 2126 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 2164
Cdd:PRK13335   125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
2697-2889 2.63e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 45.67  E-value: 2.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2697 RAEVIAkerEVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIE------DEQREKSISHQTVQQLVLEKEQALADLNSV 2770
Cdd:COG1340     31 RDELNE---ELKELAEKRDELNAQVKELREEAQELREKRDELNEkvkelkEERDELNEKLNELREELDELRKELAELNKA 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2771 EKSLADLFRRYEKM--------------KEVLEGFRKNEEVLK--KCAQEYLSRVKKEEQRYQALKVHAE---------- 2824
Cdd:COG1340    108 GGSIDKLRKEIERLewrqqtevlspeeeKELVEKIKELEKELEkaKKALEKNEKLKELRAELKELRKEAEeihkkikela 187
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779424 2825 EKLDRANAEIAQVRGKaqqeqaayQASLRKEqlrVDALERTLEQKNKEIEELTKICDELIAKMGK 2889
Cdd:COG1340    188 EEAQELHEEMIELYKE--------ADELRKE---ADELHKEIVEAQEKADELHEEIIELQKELRE 241
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2693-2834 2.79e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 2.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2693 LQVARAEVIAKEREVSEWRDKYEESRREVVEMRKI--VAEYEKtiaqmIEDEQREKSISHQTVQQlvlEKEQALADLNSV 2770
Cdd:PRK03918   621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEE-----LREEYLELSRELAGLRA---ELEELEKRREEI 692
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779424 2771 EKSLADLFRRYEKMKEVlegfRKNEEVLKKcAQEYLSRVKKEEQRYQAL-KVHAEEKLDRANAEI 2834
Cdd:PRK03918   693 KKTLEKLKEELEEREKA----KKELEKLEK-ALERVEELREKVKKYKALlKERALSKVGEIASEI 752
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2692-2876 3.45e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 3.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2692 ALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKI----------------VAEYEKTIAQmIEDEQREKSISHQTVQQ 2755
Cdd:COG4913    611 KLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAE-LEAELERLDASSDDLAA 689
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2756 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIA 2835
Cdd:COG4913    690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD-RLEAAEDLARLELRALLEERFAAALGDAVERELR 768
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1039779424 2836 QvrgkaqqeqaayqaSLRKeqlRVDALERTLEQKNKEIEEL 2876
Cdd:COG4913    769 E--------------NLEE---RIDALRARLNRAEEELERA 792
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1748-2120 3.53e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 3.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 1748 PPEPDESKDEKLHLVAPEELLSDRK-------SPGPGPATLPSVPEACVPKGFPAEARDLGGVESIPGTDDVIQPAAPVD 1820
Cdd:PHA03307    79 APANESRSTPTWSLSTLAPASPAREgsptppgPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGAS 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 1821 PGHPP--LADSSHHGDAVSSVSTHLTVQSASPSAARASPAPLAPEHTASAPSA-AGPGVEVTPTASPQHLAKNEPRSSDS 1897
Cdd:PHA03307   159 PAAVAsdAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSpISASASSPAPAPGRSAADDAGASSSD 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 1898 EEAFETPESTTPVKAPPAPPPpppevtpepevidPPAPEEPGCISEPPVVVPDGPRSSESVEGSPFRPSHSSSAVFDEDK 1977
Cdd:PHA03307   239 SSSSESSGCGWGPENECPLPR-------------PAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGS 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 1978 PIASSGTYNLDfdsielvdnFQSLEPCSADSKGQECKVSTRrksTESVPPSKStLSRSLSLQaSDFDGASCPGSPEAGTL 2057
Cdd:PHA03307   306 GPAPSSPRASS---------SSSSSRESSSSSTSSSSESSR---GAAVSPGPS-PSRSPSPS-RPPPPADPSSPRKRPRP 371
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779424 2058 TTDACGTGSNSASSTLKRTKKTRPPSLKKKQAT-KKPTETPPVKETQQEPGEESPVPSEEHLAP 2120
Cdd:PHA03307   372 SRAPSSPAASAGRPTRRRARAAVAGRARRRDATgRFPAGRPRPSPLDAGAASGAFYARYPLLTP 435
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2688-2838 5.44e-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: 45.83  E-value: 5.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2688 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM---IEDEQREKSISHQTVQQLVLEKEQAL 2764
Cdd:TIGR02169  340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYrekLEKLKREINELKRELDRLQEELQRLS 419
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779424 2765 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKvhaeEKLDRANAEIAQVR 2838
Cdd:TIGR02169  420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK----EEYDRVEKELSKLQ 489
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2683-2875 1.89e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2683 LFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM----------IEDEQREKSISHQT 2752
Cdd:COG4372     37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAqaelaqaqeeLESLQEEAEELQEE 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2753 VQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLkkcaQEYLSRVKKEEQRYqaLKVHAEEKLDRANA 2832
Cdd:COG4372    117 LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL----QEELAALEQELQAL--SEAEAEQALDELLK 190
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1039779424 2833 EIAqvRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEE 2875
Cdd:COG4372    191 EAN--RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2694-2875 2.23e-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: 42.98  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2694 QVARAEVIAKEREVSEWRDK-YEESRREvvEMRkiVAEYEKTIAQ---MIEDEQREKSISHQTVQQLVL----------- 2758
Cdd:pfam13868  126 RQLREEIDEFNEEQAEWKELeKEEEREE--DER--ILEYLKEKAEreeEREAEREEIEEEKEREIARLRaqqekaqdeka 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2759 EKEQALADLNSVE-------KSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYlsRVKKEEQRYQALKVHAE-EKLDRA 2830
Cdd:pfam13868  202 ERDELRAKLYQEEqerkerqKEREEAEKKARQRQELQQAREEQIELKERRLAEE--AEREEEEFERMLRKQAEdEEIEQE 279
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1039779424 2831 NAEiaQVRGKAQQEQAAYQASLR-KEQLRVDALERTLEQKNKEIEE 2875
Cdd:pfam13868  280 EAE--KRRMKRLEHRRELEKQIEeREEQRAAEREEELEEGERLREE 323
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
2675-2884 2.44e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 43.29  E-value: 2.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2675 EVEKppgllfQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQR--EKSISHQT 2752
Cdd:PRK04778   307 YVEK------NSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERiaEQEIAYSE 380
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2753 VQqlvlekeqalADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLS-------RVKKEE-----QRYQALK 2820
Cdd:PRK04778   381 LQ----------EELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNklheikrYLEKSNlpglpEDYLEMF 450
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779424 2821 VHAEEKLDRANAEIAQVRgkaqqeqaayqaslrkeqLRVDALERTLEQKNKEIEELTKICDELI 2884
Cdd:PRK04778   451 FEVSDEIEALAEELEEKP------------------INMEAVNRLLEEATEDVETLEEETEELV 496
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
2706-2878 2.54e-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: 43.47  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2706 EVSEWRDKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMK 2785
Cdd:TIGR04523  315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQ-LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2786 EVLEG-FRKNEEV-------LKKCAQEYLSrVKKEEQRYQALKVHAEEKLDRANAEIA----------QVRGKAQQEQAA 2847
Cdd:TIGR04523  394 NDLESkIQNQEKLnqqkdeqIKKLQQEKEL-LEKEIERLKETIIKNNSEIKDLTNQDSvkeliiknldNTRESLETQLKV 472
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1039779424 2848 YQASLRKEQLRVDALERTLEQKNKEIEELTK 2878
Cdd:TIGR04523  473 LSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
PTZ00121 PTZ00121
MAEBL; Provisional
2688-2886 3.15e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2688 DLDSALQVARAEVIAKEREV---------SEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVL 2758
Cdd:PTZ00121  1282 ELKKAEEKKKADEAKKAEEKkkadeakkkAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2759 EKEQALAD--LNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEE--KLDRANAEI 2834
Cdd:PTZ00121  1362 AEEKAEAAekKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEEkkKADEAKKKA 1440
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039779424 2835 AQVRgKAQQEQAAYQASLRKEQLRVDALE-RTLEQKNKEIEELTKiCDELIAK 2886
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 ...
2708-2886 4.16e-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: 42.70  E-value: 4.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2708 SEWRDKYEESRREVVEMRKIVAEyEKTIAQMIEDEQREKSISHQTVQQLVLEKEQaladlnsVEKSLADLFRRYEKMKev 2787
Cdd:TIGR04523  482 QNLEQKQKELKSKEKELKKLNEE-KKELEEKVKDLTKKISSLKEKIEKLESEKKE-------KESKISDLEDELNKDD-- 551
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2788 legFRKNEEVLKKCAQEYLSRVKKEEQRYQALKV---HAEEKLDRANAEIAQVR------GKAQQEQAAYQASLRKEQLR 2858
Cdd:TIGR04523  552 ---FELKKENLEKEIDEKNKEIEELKQTQKSLKKkqeEKQELIDQKEKEKKDLIkeieekEKKISSLEKELEKAKKENEK 628
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1039779424 2859 VDALERTLEQK----NKEIEELTKICDELIAK 2886
Cdd:TIGR04523  629 LSSIIKNIKSKknklKQEVKQIKETIKEIRNK 660
PRK12704 PRK12704
phosphodiesterase; Provisional
2696-2836 4.35e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 4.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2696 ARAEVIAKEREVsEWRDKYEESR----REVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVE 2771
Cdd:PRK12704    49 KEAEAIKKEALL-EAKEEIHKLRnefeKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE 127
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779424 2772 KSLADLFRRYEKMKEVLE---GFRKNE-------EVLKKCAQEYLSRVKKEEQRyqalkvhAEEKLDR-ANAEIAQ 2836
Cdd:PRK12704   128 KKEEELEELIEEQLQELErisGLTAEEakeilleKVEEEARHEAAVLIKEIEEE-------AKEEADKkAKEILAQ 196
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
2727-2876 4.39e-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: 41.05  E-value: 4.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2727 IVAEYEKTIAQMiedeqrEKSISHQTVQQLVL------EKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKK 2800
Cdd:pfam13851    2 LMKNHEKAFNEI------KNYYNDITRNNLELikslkeEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2801 CAQEYL----------SRVKKEEQRYQALKVHAEEKL--------------DRANAEIAQVRGKaqqeqaayqaSLRKEQ 2856
Cdd:pfam13851   76 QLENYEkdkqslknlkARLKVLEKELKDLKWEHEVLEqrfekvererdelyDKFEAAIQDVQQK----------TGLKNL 145
                          170       180
                   ....*....|....*....|...
gi 1039779424 2857 L---RVDALERTLEQKNKEIEEL 2876
Cdd:pfam13851  146 LlekKLQALGETLEKKEAQLNEV 168
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2697-2882 5.39e-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: 42.65  E-value: 5.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2697 RAEVIAKEREVsewrdkyEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTV--QQLVLEKEQALADLNSVEKSL 2774
Cdd:pfam02463  185 LAELIIDLEEL-------KLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLneERIDLLQELLRDEQEEIESSK 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2775 ADLFRRYEKMKEVLEGFRKNEEVLK-----------KCAQEYLSRVKKEEQRYQALK--VHAEEKLDRANAEIAQVRGKA 2841
Cdd:pfam02463  258 QEIEKEEEKLAQVLKENKEEEKEKKlqeeelkllakEEEELKSELLKLERRKVDDEEklKESEKEKKKAEKELKKEKEEI 337
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1039779424 2842 QQEQAAYQASLRKEQL----RVDALERTLEQKNKEIEELTKICDE 2882
Cdd:pfam02463  338 EELEKELKELEIKREAeeeeEEELEKLQEKLEQLEEELLAKKKLE 382
PTZ00121 PTZ00121
MAEBL; Provisional
2692-2883 5.54e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 5.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2692 ALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIE-DEQREKSISHQTVQQLVLEKEQALADLNSV 2770
Cdd:PTZ00121  1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2771 EKSlADLFRRYEKMKEVLEGFRKNEEVLKKCAQ----EYLSRVKKEEQRYQALKVHAEE--KLDRANAEIAQVRGKAQQE 2844
Cdd:PTZ00121  1424 KKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEakkaEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEA 1502
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1039779424 2845 QAAYQASLRKEQLRvDALERTLEQKNKEIEELTKiCDEL 2883
Cdd:PTZ00121  1503 KKAAEAKKKADEAK-KAEEAKKADEAKKAEEAKK-ADEA 1539
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
2688-2887 5.90e-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: 41.06  E-value: 5.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2688 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEyektiaqmIEDEQREKSISHQTVQQLVLEKEQALA-- 2765
Cdd:COG1579     14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED--------LEKEIKRLELEIEEVEARIKKYEEQLGnv 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2766 ----DLNSVEKSLADLfrryEKMKEVLEgfrknEEVLkkcaqeylsrvkkeeqryqalkvHAEEKLDRANAEIAQVRGKA 2841
Cdd:COG1579     86 rnnkEYEALQKEIESL----KRRISDLE-----DEIL-----------------------ELMERIEELEEELAELEAEL 133
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1039779424 2842 QQeqaayqaslRKEQLR--VDALERTLEQKNKEIEELTKICDELIAKM 2887
Cdd:COG1579    134 AE---------LEAELEekKAELDEELAELEAELEELEAEREELAAKI 172
PRK01156 PRK01156
chromosome segregation protein; Provisional
2697-2875 6.11e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.20  E-value: 6.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2697 RAEVIAKER-EVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLA 2775
Cdd:PRK01156   347 RYDDLNNQIlELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2776 DLFRRYEKMKEVLEGFRKNEEVLK---KC-------AQEYLSRVKKEeqrYQALKVHAEEKLDRANAEIAQVRGKAQQEQ 2845
Cdd:PRK01156   427 SLNQRIRALRENLDELSRNMEMLNgqsVCpvcgttlGEEKSNHIINH---YNEKKSRLEEKIREIEIEVKDIDEKIVDLK 503
                          170       180       190
                   ....*....|....*....|....*....|
gi 1039779424 2846 AAYQASLRKEQLRVDALERTLEQKNKEIEE 2875
Cdd:PRK01156   504 KRKEYLESEEINKSINEYNKIESARADLED 533
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2753-2877 6.22e-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: 6.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2753 VQQLVLEKEQALADLNsvekSLADLFRRYEKMKEVLEGFRKNEEVL---KKCAQEYLS-RVKKEEQRYQALKVH---AEE 2825
Cdd:COG4913    213 VREYMLEEPDTFEAAD----ALVEHFDDLERAHEALEDAREQIELLepiRELAERYAAaRERLAELEYLRAALRlwfAQR 288
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039779424 2826 KLDRANAEIAQVRgkaqqeqaayqASLRKEQLRVDALERTLEQKNKEIEELT 2877
Cdd:COG4913    289 RLELLEAELEELR-----------AELARLEAELERLEARLDALREELDELE 329
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2747-2889 6.73e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 6.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2747 SISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEgfRKNEEVLKkcAQEYLSRVKKEEQRYQALKVHAEEK 2826
Cdd:COG4372     27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELE--QARSELEQ--LEEELEELNEQLQAAQAELAQAQEE 102
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779424 2827 LDRANAEIAQVRGKAQQEQAAYQA-SLRKEQL--RVDALERTLEQKNKEIEELTKICDELIAKMGK 2889
Cdd:COG4372    103 LESLQEEAEELQEELEELQKERQDlEQQRKQLeaQIAELQSEIAEREEELKELEEQLESLQEELAA 168
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
2689-2883 8.33e-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: 8.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2689 LDSALQVARAEViakeREVSEW-RDKYEESRREVVEMRKIVAEYEKtiAQMIEDEQREKSISHQTVQQLVLEKEQALADL 2767
Cdd:COG3206    162 LEQNLELRREEA----RKALEFlEEQLPELRKELEEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2768 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVlkkcaQEYLSRVKKEEQRYQALKVHAEEK---LDRANAEIAQVRGKAQQE 2844
Cdd:COG3206    236 AEAEARLAALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQE 310
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1039779424 2845 QAAYQASLRKE----QLRVDALERTLEQKNKEIEELTKICDEL 2883
Cdd:COG3206    311 AQRILASLEAElealQAREASLQAQLAQLEARLAELPELEAEL 353
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2694-2886 9.51e-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: 41.06  E-value: 9.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2694 QVARAEVIAKEREvsewrdkyEESRREVVEMRKivaEYEKTIAQMIEDEQREKSISHQTVQQLV-----------LEKEQ 2762
Cdd:pfam13868   27 QIAEKKRIKAEEK--------EEERRLDEMMEE---ERERALEEEEEKEEERKEERKRYRQELEeqieereqkrqEEYEE 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2763 ALADLNSV--------EKSLADLFRRYEKMKEVLEGFRK-NEEVLKKCAQEYLsRVKKEEQRYQAlkvHAEEKLDRANAE 2833
Cdd:pfam13868   96 KLQEREQMdeiveriqEEDQAEAEEKLEKQRQLREEIDEfNEEQAEWKELEKE-EEREEDERILE---YLKEKAEREEER 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039779424 2834 IAQVRGKAqqeqaayqaslRKEQLRVDALERTLEQKNKEIEELtkicDELIAK 2886
Cdd:pfam13868  172 EAEREEIE-----------EEKEREIARLRAQQEKAQDEKAER----DELRAK 209
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
2706-2829 9.90e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 40.66  E-value: 9.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779424 2706 EVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIE--DEQREKSIS-HQTVQqlvlEKEQALADLNsveKSLADLFRRYE 2782
Cdd:COG1340    168 ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKeaDELRKEADElHKEIV----EAQEKADELH---EEIIELQKELR 240
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1039779424 2783 KMKEVLEGFRKNEEVLKKcaqeylsrvKKEEQRYQALKVHAEEKLDR 2829
Cdd:COG1340    241 ELRKELKKLRKKQRALKR---------EKEKEELEEKAEEIFEKLKK 278
 
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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