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Conserved domains on  [gi|166197652|ref|NP_075806|]
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nuclear distribution protein nudE homolog 1 isoform a [Mus musculus]

Protein Classification

SPEC and NUDE_C domain-containing protein( domain architecture ID 10522326)

SPEC and NUDE_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NUDE_C pfam04880
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ...
 134-309 3.41e-55

NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved region of the NUDE proteins. NUDE proteins are involved in nuclear migration.


:

Pssm-ID: 461464 [Multi-domain]  Cd Length: 169  Bit Score: 178.06  E-value: 3.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  134 SLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ------DKPRTPMPGSGQAKRTD 203
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKlrnllmRSPSTPSLQTLEIFDRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  204 MAVQATgsvpSTPVAHRGPSSGLNTpgmFRRGldsSTSGTPLTPAARISAlnivgDLLRKVGALESKLASCRNFMYDQSP 283
Cdd:pfam04880  81 PAVQAV----SSPVIATPPEKSFNS---LRTG---SETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNA 145

                         170       180
                  ....*....|....*....|....*.
gi 166197652  284 SRtsgpasgRGTKNRDGVDRRPGSTS 309
Cdd:pfam04880 146 SR-------RGNSRSLYGSRPPTKFA 164
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-186 5.44e-09

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 5.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    26 KQRAENTQEELREFQEGSREYEAELEAQLQQIEtRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   106 -------IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168  818 eaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897


                   ....*...
gi 166197652   179 ELAVQQKQ 186
Cdd:TIGR02168  898 ELSEELRE 905
 
Name Accession Description Interval E-value
NUDE_C pfam04880
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ...
 134-309 3.41e-55

NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved region of the NUDE proteins. NUDE proteins are involved in nuclear migration.


Pssm-ID: 461464 [Multi-domain]  Cd Length: 169  Bit Score: 178.06  E-value: 3.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  134 SLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ------DKPRTPMPGSGQAKRTD 203
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKlrnllmRSPSTPSLQTLEIFDRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  204 MAVQATgsvpSTPVAHRGPSSGLNTpgmFRRGldsSTSGTPLTPAARISAlnivgDLLRKVGALESKLASCRNFMYDQSP 283
Cdd:pfam04880  81 PAVQAV----SSPVIATPPEKSFNS---LRTG---SETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNA 145

                         170       180
                  ....*....|....*....|....*.
gi 166197652  284 SRtsgpasgRGTKNRDGVDRRPGSTS 309
Cdd:pfam04880 146 SR-------RGNSRSLYGSRPPTKFA 164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-186 5.44e-09

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: 57.76  E-value: 5.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    26 KQRAENTQEELREFQEGSREYEAELEAQLQQIEtRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   106 -------IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168  818 eaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897


                   ....*...
gi 166197652   179 ELAVQQKQ 186
Cdd:TIGR02168  898 ELSEELRE 905
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-187 1.43e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  26 KQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477


                 ..
gi 166197652 186 QD 187
Cdd:COG1196  478 AL 479
mukB PRK04863
chromosome partition protein MukB;
41-186 6.58e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 48.03  E-value: 6.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   41 EGSREYEAELEAQLQQIETRnrdLLSENNRLRMElESVKEKFE------------MQHSEGYRQISALEDDLAQTKAIKD 108
Cdd:PRK04863  438 DNAEDWLEEFQAKEQEATEE---LLSLEQKLSVA-QAAHSQFEqayqlvrkiageVSRSEAWDVARELLRRLREQRHLAE 513

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  109 QLQKY---IRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:PRK04863  514 QLQQLrmrLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLE 589


                  .
gi 166197652  186 Q 186
Cdd:PRK04863  590 Q 590
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 26-253 2.37e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  26 KQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLL---SENNRLRMELESvkekfemqhsegyRQISALEDDLAQ 102
Cdd:COG3883   57 QAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsgGSVSYLDVLLGS-------------ESFSDFLDRLSA 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652 103 TKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAV 182
Cdd:COG3883  124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166197652 183 QQKQDKPRTPMPGSGQAKRTDMAVQATGSVPSTPVAHRGPSSGLNTPGMFRRGLDSSTSGTPLTPAARISA 253
Cdd:COG3883  204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 20-211 2.59e-05

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 45.98  E-value: 2.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    20 DLAMTYKQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEMQHSE------GYRQ- 92
Cdd:pfam12128  643 FARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREartekqAYWQv 722

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    93 -ISALEDDLAQTKAIKDQLQ------------KYIREL------EQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLE 153
Cdd:pfam12128  723 vEGALDAQLALLKAAIAARRsgakaelkaletWYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQ 802

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 166197652   154 SE-LDEKENLLESVQRLKDEARDLRQELAVQQKQDKPRTPMPGSGQAKRTDMAVQATGS 211
Cdd:pfam12128  803 ETwLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSEN 861
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 19-188 4.67e-05

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 44.67  E-value: 4.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  19 RDLAMTYKQRAENTQEELREFQEGSREYeaelEAQLQQIETRNRDLLSENNRL--RMELESVKEkfemqhsegyrQISAL 96
Cdd:cd22656  127 LKEAKKYQDKAAKVVDKLTDFENQTEKD----QTALETLEKALKDLLTDEGGAiaRKEIKDLQK-----------ELEKL 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  97 EDDLAqtKAIKDQLQKYIRELEQANDDLERAKR------ATIMSLEDFEQRLNQAIE-----RNAF--LESELDEKENLL 163
Cdd:cd22656  192 NEEYA--AKLKAKIDELKALIADDEAKLAAALRliadltAADTDLDNLLALIGPAIPaleklQGAWqaIATDLDSLKDLL 269

                        170       180
                 ....*....|....*....|....*
gi 166197652 164 ESVQRlkDEARDLRQELAVQQKQDK 188
Cdd:cd22656  270 EDDIS--KIPAAILAKLELEKAIEK 292
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
 142-187 3.19e-03

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 38.81  E-value: 3.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 166197652 142 LNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQD 187
Cdd:PRK13922  71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNLKESLD 116
 
Name Accession Description Interval E-value
NUDE_C pfam04880
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ...
 134-309 3.41e-55

NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved region of the NUDE proteins. NUDE proteins are involved in nuclear migration.


Pssm-ID: 461464 [Multi-domain]  Cd Length: 169  Bit Score: 178.06  E-value: 3.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  134 SLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ------DKPRTPMPGSGQAKRTD 203
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKlrnllmRSPSTPSLQTLEIFDRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  204 MAVQATgsvpSTPVAHRGPSSGLNTpgmFRRGldsSTSGTPLTPAARISAlnivgDLLRKVGALESKLASCRNFMYDQSP 283
Cdd:pfam04880  81 PAVQAV----SSPVIATPPEKSFNS---LRTG---SETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNA 145

                         170       180
                  ....*....|....*....|....*.
gi 166197652  284 SRtsgpasgRGTKNRDGVDRRPGSTS 309
Cdd:pfam04880 146 SR-------RGNSRSLYGSRPPTKFA 164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-186 5.44e-09

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: 57.76  E-value: 5.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    26 KQRAENTQEELREFQEGSREYEAELEAQLQQIEtRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   106 -------IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168  818 eaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897


                   ....*...
gi 166197652   179 ELAVQQKQ 186
Cdd:TIGR02168  898 ELSEELRE 905
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-187 1.43e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  26 KQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477


                 ..
gi 166197652 186 QD 187
Cdd:COG1196  478 AL 479
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-186 2.43e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 2.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  27 QRAENTQEELREFQEGSREYEAELEAQLQQIE---TRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISALEDDLAQT 103
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAELARLEqdiARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652 104 KAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQ 183
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429


                 ...
gi 166197652 184 QKQ 186
Cdd:COG1196  430 LAE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 12-188 3.60e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 3.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  12 EEETNYWRDLAMTYKQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKF---EMQHSE 88
Cdd:COG1196  220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyelLAELAR 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  89 GYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQR 168
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                        170       180
                 ....*....|....*....|
gi 166197652 169 LKDEARDLRQELAVQQKQDK 188
Cdd:COG1196  380 ELEELAEELLEALRAAAELA 399
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
27-190 3.66e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.77  E-value: 3.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  27 QRAENTQEELREFQEGSREYEAELEAQLQQIET--RNRDLLSENNRLRMELESVKEKFEmqhsEGYRQISALEDDLAQTK 104
Cdd:COG4717   91 AELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE----ELEERLEELRELEEELE 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652 105 AIKDQLQKYIRELEQANDDLERAKRATimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQ 184
Cdd:COG4717  167 ELEAELAELQEELEELLEQLSLATEEE---LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243


                 ....*.
gi 166197652 185 KQDKPR 190
Cdd:COG4717  244 RLKEAR 249
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 9-188 4.90e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 4.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   9 ESEEEETNYWRDLAMTYKQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEMQHSE 88
Cdd:COG1196  298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  89 GYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQR 168
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        170       180
                 ....*....|....*....|
gi 166197652 169 LKDEARDLRQELAVQQKQDK 188
Cdd:COG1196  458 EEALLELLAELLEEAALLEA 477
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
27-210 1.19e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   27 QRAENTQEELREFQEGSREYEAELEAQLQQIE-TRNRDLLSENNRLRMELESVKEKFEMQHSE--------GYRQISALE 97
Cdd:COG4913   265 AAARERLAELEYLRAALRLWFAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDEleaqirgnGGDRLEQLE 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   98 DDLAQTKAIKDQLQkyiRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEN----LLESVQRLKDEA 173
Cdd:COG4913   345 REIERLERELEERE---RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRREL 421

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 166197652  174 RDLRQELAVQQKQdkpRTPMPGSGQAKRTDMAvQATG 210
Cdd:COG4913   422 RELEAEIASLERR---KSNIPARLLALRDALA-EALG 454
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 34-186 1.46e-07

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: 53.14  E-value: 1.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    34 EELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKF---EMQHSEGYRQISALEDDLAQTKAIKDQL 110
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166197652   111 QKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEARDLRQELAVQQKQ 186
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR---AELTLLNEEAANLRERLESLERR 832
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 24-186 2.02e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  24 TYKQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRM------ELESVKEKFEMQHSEGYRQISALE 97
Cdd:COG1196  243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaelaRLEQDIARLEERRRELEERLEELE 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  98 DDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLR 177
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402


                 ....*....
gi 166197652 178 QELAVQQKQ 186
Cdd:COG1196  403 EELEEAEEA 411
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-186 1.00e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  26 KQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEMQHSEgyrqISALEDDLAQTKA 105
Cdd:COG1196  297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEA 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452


                 .
gi 166197652 186 Q 186
Cdd:COG1196  453 E 453
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 30-188 1.47e-06

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: 50.02  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   30 ENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRL---RMELESVK-EKFEMQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLnqlKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQN 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  106 IKDQLQKYIRELEQANDDLERakraTIMSLEDFEQRLNQAI-ERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQ 184
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKK----ELTNSESENSEKQRELeEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404


                  ....
gi 166197652  185 KQDK 188
Cdd:TIGR04523 405 KLNQ 408
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
47-208 1.59e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  47 EAELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEMQHsegyRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLER 126
Cdd:COG4717   48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREELEKLEK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652 127 AKRA--TIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQDKPRTPMPGSGQAKRTDM 204
Cdd:COG4717  124 LLQLlpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203


                 ....
gi 166197652 205 AVQA 208
Cdd:COG4717  204 LQQR 207
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-188 1.86e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  27 QRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKF---EMQHSEGYRQISALEDDLAQT 103
Cdd:COG1196  333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELleaLRAAAELAAQLEELEEAEEAL 412

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652 104 KAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQ 183
Cdd:COG1196  413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492


                 ....*
gi 166197652 184 QKQDK 188
Cdd:COG1196  493 LLLLL 497
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
24-186 1.99e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.63  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  24 TYKQRAENTQEELREFQEGSREYE------------AELEAQLQQIETRNRDLLSENNRLRMELESVKEkfEMQHSEGYR 91
Cdd:COG3206  186 ELRKELEEAEAALEEFRQKNGLVDlseeaklllqqlSELESQLAEARAELAEAEARLAALRAQLGSGPD--ALPELLQSP 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  92 QISALEDDLAQTKA-IKDQLQKY------IRELEQANDDLERAKRATI-MSLEDFEQRLNQAIERNAFLESELDEKENLL 163
Cdd:COG3206  264 VIQQLRAQLAELEAeLAELSARYtpnhpdVIALRAQIAALRAQLQQEAqRILASLEAELEALQAREASLQAQLAQLEARL 343

                        170       180
                 ....*....|....*....|...
gi 166197652 164 ESVQRLKDEARDLRQELAVQQKQ 186
Cdd:COG3206  344 AELPELEAELRRLEREVEVAREL 366
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-180 2.02e-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: 49.67  E-value: 2.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    27 QRAENTQEELREFQEGS-----REYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKfEMQHSEGYRQISALEDDLA 101
Cdd:TIGR02168  213 ERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELEEEIEELQKELY 291

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166197652   102 QTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-181 2.70e-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: 49.28  E-value: 2.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    26 KQRAENTQEELREFQEGSREYEAELEAQLQQIEtRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIE-ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL------------ESVQRLKDEA 173
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaealenkieDDEEEARRRL 974


                   ....*...
gi 166197652   174 RDLRQELA 181
Cdd:TIGR02168  975 KRLENKIK 982
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 26-186 4.72e-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: 47.84  E-value: 4.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  26 KQRAENTQEELREFQEGSREYEA---ELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQ---------- 92
Cdd:COG4942   47 KKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalll 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  93 ----ISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQR 168
Cdd:COG4942  127 spedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206

                        170
                 ....*....|....*...
gi 166197652 169 LKDEARDLRQELAVQQKQ 186
Cdd:COG4942  207 ELAELAAELAELQQEAEE 224
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 8-176 5.54e-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: 48.13  E-value: 5.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652     8 FESEEEETNYWRDLAMTYKQRAENTQEELREFQEGSREYEAELE---AQLQQIETRNRDLLSENNRLRMELESVKEKFEM 84
Cdd:TIGR02168  353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAslnNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    85 QhsegyrQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLE 164
Cdd:TIGR02168  433 A------ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506

                          170
                   ....*....|..
gi 166197652   165 SVQRLKDEARDL 176
Cdd:TIGR02168  507 GVKALLKNQSGL 518
mukB PRK04863
chromosome partition protein MukB;
41-186 6.58e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 48.03  E-value: 6.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   41 EGSREYEAELEAQLQQIETRnrdLLSENNRLRMElESVKEKFE------------MQHSEGYRQISALEDDLAQTKAIKD 108
Cdd:PRK04863  438 DNAEDWLEEFQAKEQEATEE---LLSLEQKLSVA-QAAHSQFEqayqlvrkiageVSRSEAWDVARELLRRLREQRHLAE 513

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  109 QLQKY---IRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:PRK04863  514 QLQQLrmrLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLE 589


                  .
gi 166197652  186 Q 186
Cdd:PRK04863  590 Q 590
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1-186 6.60e-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: 48.14  E-value: 6.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652     1 MEDSGKTFESEEEETNYWRDLAMTYKQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLlsenNRLRMELESVK- 79
Cdd:TIGR02169  711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEa 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    80 --------------EKFEMQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLE--------------RAKRAT 131
Cdd:TIGR02169  787 rlshsripeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKeqiksiekeienlnGKKEEL 866

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 166197652   132 IMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQ 186
Cdd:TIGR02169  867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 9-173 6.95e-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: 47.76  E-value: 6.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652     9 ESEEEETNYWRDLAMTYKQRAENTQEELREFQEGSREYEA-----------------ELEAQLQQIETRNRDLLSENNRL 71
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAalrdlesrlgdlkkerdELEAQLRELERKIEELEAQIEKK 915

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    72 RMELESVKEKFEMQHSEgyrqISALEDDLAQTKAIK------DQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQA 145
Cdd:TIGR02169  916 RKRLSELKAKLEALEEE----LSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDEL 991

                          170       180
                   ....*....|....*....|....*...
gi 166197652   146 IERNAFLESELDEKENLLESVQRLKDEA 173
Cdd:TIGR02169  992 KEKRAKLEEERKAILERIEEYEKKKREV 1019
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-181 9.54e-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: 47.36  E-value: 9.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652     7 TFESEEEETNYWRDLAMTYKQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEM-- 84
Cdd:TIGR02168  299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEle 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    85 QHSEGYR---------------QISALEDDLAQtkaIKDQLQKYIRELEQANDDLERAKRATI-MSLEDFEQRLNQAIER 148
Cdd:TIGR02168  379 EQLETLRskvaqlelqiaslnnEIERLEARLER---LEDRRERLQQEIEELLKKLEEAELKELqAELEELEEELEELQEE 455

                          170       180       190
                   ....*....|....*....|....*....|...
gi 166197652   149 NAFLESELDEKENLLESVQRLKDEARDLRQELA 181
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELAQLQ 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-200 1.07e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652     1 MEDSGKTFESEEEETNYWRDLAMTYKQRAENTQEELREFQEGSREYEA---ELEAQLQQIETRNRDLLSENNRLRMELES 77
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESkrsELRRELEELREKLAQLELRLEGLEVRIDN 940

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    78 VKEKFemqhSEGYRqiSALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQrLNqaiERNAFLESELD 157
Cdd:TIGR02168  941 LQERL----SEEYS--LTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEE-LK---ERYDFLTAQKE 1010

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 166197652   158 E----KENLLESVQRLKDEARDLRQELAVQQKQDKPRT--PMPGSGQAK 200
Cdd:TIGR02168 1011 DlteaKETLEEAIEEIDREARERFKDTFDQVNENFQRVfpKLFGGGEAE 1059
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 9-187 1.60e-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: 46.97  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652     9 ESEEEETNYWRDLAMTYKQRAEnTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRmELESVKEKFEMQHSE 88
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA-NLERQLEELEAQLEE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    89 GYRQISALEDDLAQTKAIKDQLQKYIRELEQAND-------DLERAKRATIMSLEDFEQRLNQAIERNAFLESEL----D 157
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLEAELEeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIerleA 407

                          170       180       190
                   ....*....|....*....|....*....|
gi 166197652   158 EKENLLESVQRLKDEARDLRQELAVQQKQD 187
Cdd:TIGR02168  408 RLERLEDRRERLQQEIEELLKKLEEAELKE 437
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 49-187 1.73e-05

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: 46.55  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   49 ELEAQLQQIETRNRDLLSE-----NNRLRMELESVKEKF---EMQHSEGYRQISALEDDLAQTKAIKDQL----QKYIRE 116
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLeeiQNQISQNNKIISQLNEQISQLKKELTNSesenSEKQRE 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  117 LEQANDDLERAKRA------TIMSLEDFEQRLNQAIERNAFLESELD--------EKENLLESVQRLKDEARDLRQELAV 182
Cdd:TIGR04523 365 LEEKQNEIEKLKKEnqsykqEIKNLESQINDLESKIQNQEKLNQQKDeqikklqqEKELLEKEIERLKETIIKNNSEIKD 444


                  ....*
gi 166197652  183 QQKQD 187
Cdd:TIGR04523 445 LTNQD 449
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 26-253 2.37e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  26 KQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLL---SENNRLRMELESvkekfemqhsegyRQISALEDDLAQ 102
Cdd:COG3883   57 QAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsgGSVSYLDVLLGS-------------ESFSDFLDRLSA 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652 103 TKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAV 182
Cdd:COG3883  124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166197652 183 QQKQDKPRTPMPGSGQAKRTDMAVQATGSVPSTPVAHRGPSSGLNTPGMFRRGLDSSTSGTPLTPAARISA 253
Cdd:COG3883  204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 20-211 2.59e-05

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 45.98  E-value: 2.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    20 DLAMTYKQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEMQHSE------GYRQ- 92
Cdd:pfam12128  643 FARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREartekqAYWQv 722

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    93 -ISALEDDLAQTKAIKDQLQ------------KYIREL------EQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLE 153
Cdd:pfam12128  723 vEGALDAQLALLKAAIAARRsgakaelkaletWYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQ 802

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 166197652   154 SE-LDEKENLLESVQRLKDEARDLRQELAVQQKQDKPRTPMPGSGQAKRTDMAVQATGS 211
Cdd:pfam12128  803 ETwLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSEN 861
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 26-186 4.45e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  26 KQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRmELESVKEKFEMQHSEGYRQISALEDDLAQtka 105
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-ALEQELAALEAELAELEKEIAELRAELEA--- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652 106 IKDQLQKYIRELEQANddlERAKRATIMSLEDFeqrlNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG4942  102 QKEELAELLRALYRLG---RQPPLALLLSPEDF----LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174


                 .
gi 166197652 186 Q 186
Cdd:COG4942  175 E 175
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 19-188 4.67e-05

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 44.67  E-value: 4.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  19 RDLAMTYKQRAENTQEELREFQEGSREYeaelEAQLQQIETRNRDLLSENNRL--RMELESVKEkfemqhsegyrQISAL 96
Cdd:cd22656  127 LKEAKKYQDKAAKVVDKLTDFENQTEKD----QTALETLEKALKDLLTDEGGAiaRKEIKDLQK-----------ELEKL 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  97 EDDLAqtKAIKDQLQKYIRELEQANDDLERAKR------ATIMSLEDFEQRLNQAIE-----RNAF--LESELDEKENLL 163
Cdd:cd22656  192 NEEYA--AKLKAKIDELKALIADDEAKLAAALRliadltAADTDLDNLLALIGPAIPaleklQGAWqaIATDLDSLKDLL 269

                        170       180
                 ....*....|....*....|....*
gi 166197652 164 ESVQRlkDEARDLRQELAVQQKQDK 188
Cdd:cd22656  270 EDDIS--KIPAAILAKLELEKAIEK 292
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 95-186 4.86e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 4.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  95 ALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEAR 174
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEIA 93

                         90
                 ....*....|..
gi 166197652 175 DLRQELAVQQKQ 186
Cdd:COG4942   94 ELRAELEAQKEE 105
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 26-174 8.56e-05

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: 43.37  E-value: 8.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  26 KQRAENTQEELREFQEGSREYEAELEAQLQQIEtrnrDLLSENNRLRMELESVKEKFE-----MQHSEGYRQISALEDDL 100
Cdd:COG1579   23 EHRLKELPAELAELEDELAALEARLEAAKTELE----DLEKEIKRLELEIEEVEARIKkyeeqLGNVRNNKEYEALQKEI 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166197652 101 AQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEAR 174
Cdd:COG1579   99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELA 169
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 48-164 9.21e-05

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: 42.97  E-value: 9.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   48 AELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEM--QHSEGYRQISAledDLAQTKAIKDQLQKYIRELEQANDDLE 125
Cdd:pfam13851  36 AELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEElrKQLENYEKDKQ---SLKNLKARLKVLEKELKDLKWEHEVLE 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 166197652  126 RAKRATIMSLEDFEQRLNQAIE--------RNAFLESELDEKENLLE 164
Cdd:pfam13851 113 QRFEKVERERDELYDKFEAAIQdvqqktglKNLLLEKKLQALGETLE 159
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-176 1.19e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  27 QRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISALEDDLAQTKAI 106
Cdd:COG1196  682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166197652 107 KDQLQKYIRELEQANDDLE----RAkratimsLEDFEqrlnQAIERNAFLESELD----EKENLLESVQRLKDEARDL 176
Cdd:COG1196  762 LEELERELERLEREIEALGpvnlLA-------IEEYE----ELEERYDFLSEQREdleeARETLEEAIEEIDRETRER 828
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 26-177 1.25e-04

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: 43.86  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   26 KQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELEsvKEKFEMQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKK 582

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166197652  106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDE----KENLLESVQRLKDEARDLR 177
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNikskKNKLKQEVKQIKETIKEIR 658
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 34-173 1.32e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 43.79  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  34 EELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVkekfemqhsEGYRQISALEDDLaqtKAIKDQLQKY 113
Cdd:COG5185  322 EAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENI---------VGEVELSKSSEEL---DSFKDTIEST 389

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652 114 IRELEQANDDlerAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEA 173
Cdd:COG5185  390 KESLDEIPQN---QRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNEL 446
PRK14160 PRK14160
heat shock protein GrpE; Provisional
 1-185 1.38e-04

heat shock protein GrpE; Provisional


Pssm-ID: 237629 [Multi-domain]  Cd Length: 211  Bit Score: 42.43  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   1 MEDSGKTFESEEEETNywrdlamtykqraENTQEELREF--QEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESV 78
Cdd:PRK14160  14 EEDCCKENENKEEDKG-------------KEEDLEFEEIekEEIIEDSEESNEVKIEELKDENNKLKEENKKLENELEAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  79 KEKFE--MQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELeqanDDLERAKrATIMSLEDFEQRLNQAIE--RNAF--- 151
Cdd:PRK14160  81 KDRLLrtVAEYDNYRKRTAKEKEGIYSDACEDVLKELLPVL----DNLERAA-AVEGSVEDLKKGIEMTVKqfKTSLekl 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 166197652 152 ----LESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:PRK14160 156 gveeISTEGEFDPNLHNAVMHVEDENYGENEIVEVFQK 193
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 40-190 1.69e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.40  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   40 QEGSREYEAELEAQLQQIETRNRDLlsennRLRMeleSVKEKFEMQHSEGY-----------------------RQISAL 96
Cdd:COG3096   436 PENAEDYLAAFRAKEQQATEEVLEL-----EQKL---SVADAARRQFEKAYelvckiageversqawqtarellRRYRSQ 507

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   97 EDDLAQTKAIKDQLqkyiRELEQANDDLERAKRatimSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDL 176
Cdd:COG3096   508 QALAQRLQQLRAQL----AELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579

                         170
                  ....*....|....
gi 166197652  177 RQELAVQQKQDKPR 190
Cdd:COG3096   580 RSELRQQLEQLRAR 593
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
28-186 2.52e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  28 RAENTQEELREFQEGSREYEAELEAQLQQIETRnrdlLSENNRLrmeLESVKEKFEMQHSEGYRQISALEDDLAQTKAIK 107
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLRTARER----VEEAEAL---LEAGKCPECGQPVEGSPHVETIEEDRERVEELE 481

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652 108 DQLQKYIRELEQANDDLERAKratimSLEDFEQRLNQAIERNAFLESELDEKENLLES----VQRLKDEARDLRQELAVQ 183
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAE-----DLVEAEDRIERLEERREDLEELIAERRETIEEkrerAEELRERAAELEAEAEEK 556


                 ...
gi 166197652 184 QKQ 186
Cdd:PRK02224 557 REA 559
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 37-190 3.21e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  37 REFQEGSREYEAELeaQLQQIETRNRDLlsenNRLRMELESVKEKFEmqhsegyrqisALEDDLAQTKAIKDQLQKYIRE 116
Cdd:COG1196  216 RELKEELKELEAEL--LLLKLRELEAEL----EELEAELEELEAELE-----------ELEAELAELEAELEELRLELEE 278

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166197652 117 LEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQDKPR 190
Cdd:COG1196  279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 24-188 3.33e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.80  E-value: 3.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    24 TYKQRAENTQEEL-REFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISALEDDLAQ 102
Cdd:pfam15921  249 ALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQ 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   103 tkaIKDQLQKYIRELEQANDDLEraKRATIMSLEDFEQRlnqaIERNAFLEseldEKENLLESVQRLKDEARDLRQELAV 182
Cdd:pfam15921  329 ---LRSELREAKRMYEDKIEELE--KQLVLANSELTEAR----TERDQFSQ----ESGNLDDQLQKLLADLHKREKELSL 395


                   ....*.
gi 166197652   183 QQKQDK 188
Cdd:pfam15921  396 EKEQNK 401
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 25-188 3.95e-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: 42.36  E-value: 3.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    25 YKQRAENTQEELREFQEGSREYeAELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISA-LEDDLAQT 103
Cdd:TIGR02169  225 GYELLKEKEALERQKEAIERQL-ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkIGELEAEI 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   104 KAIKDQLQKYIRELEQANDDLERAK---RATIMSLEDFEQRLNQAIERNAFLESELDEKENLLE-SVQRLKD---EARDL 176
Cdd:TIGR02169  304 ASLERSIAEKERELEDAEERLAKLEaeiDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdLRAELEEvdkEFAET 383

                          170
                   ....*....|...
gi 166197652   177 RQELA-VQQKQDK 188
Cdd:TIGR02169  384 RDELKdYREKLEK 396
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
9-180 4.23e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 4.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   9 ESEEEEtnyWRDLAMTYKQRAENTQEELREFQEGSREYEAELEAqLQQIetrnRDLLSENNRLRMELESVKEKFEMQH-- 86
Cdd:PRK02224 550 EAEAEE---KREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERI----RTLLAAIADAEDEIERLREKREALAel 621

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  87 --------SEGYRQISALEDD-----LAQTKAIKDQLQKYIRELEQANDDLERAK---RATIMSLEDFEQRLNQAIERNA 150
Cdd:PRK02224 622 nderrerlAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERddlQAEIGAVENELEELEELRERRE 701

                        170       180       190
                 ....*....|....*....|....*....|
gi 166197652 151 FLESELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:PRK02224 702 ALENRVEALEALYDEAEELESMYGDLRAEL 731
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 33-184 4.58e-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: 41.98  E-value: 4.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    33 QEELREFQEGSREYEAELEAQLQQIETRNRDLlsenNRLRMELESVKEKFEmqhsEGYRQISALEDDLAQTKAIKDQLQK 112
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSDASRKIGEIEKEI----EQLEQEEEKLKERLE----ELEEDLSSLEQEIENVKSELKELEA 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   113 YIRELEQANDDLERAkratimsLEDFEQRLNQAI------------ERNAFLESELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:TIGR02169  766 RIEELEEDLHKLEEA-------LNDLEARLSHSRipeiqaelskleEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838


                   ....
gi 166197652   181 AVQQ 184
Cdd:TIGR02169  839 QEQR 842
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 26-191 6.10e-04

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: 6.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    26 KQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISALEdDLAQTKA 105
Cdd:pfam02463  148 AMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL-ELEEEYL 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   106 IKDQLQKYIRELEQANDDLERAKRATIMSLedfEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:pfam02463  227 LYLDYLKLNEERIDLLQELLRDEQEEIESS---KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL 303


                   ....*.
gi 166197652   186 QDKPRT 191
Cdd:pfam02463  304 KLERRK 309
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 21-190 6.15e-04

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: 41.65  E-value: 6.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   21 LAMTYKQRAENTQEELREFQ-EGSREYEAELE-AQLQQIETRNRDLLSENNRLRMELESVKeKFEMQHSEGYRQISALED 98
Cdd:pfam17380 342 MAMERERELERIRQEERKRElERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAAR-KVKILEEERQRKIQQQKV 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   99 DLAQTKAIKDQL-QKYIRELEQanddlERAKRATIMSLEDFEQRlnQAIERNAFLESELDEKENLLESVQRLKDEARDLR 177
Cdd:pfam17380 421 EMEQIRAEQEEArQREVRRLEE-----ERAREMERVRLEEQERQ--QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR 493

                         170
                  ....*....|...
gi 166197652  178 QELAVQQKQDKPR 190
Cdd:pfam17380 494 RKILEKELEERKQ 506
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 48-234 8.01e-04

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 40.87  E-value: 8.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   48 AELEAQLQQIETRNRDLLSENNRLRMELEsvkeKFEMQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERA 127
Cdd:pfam00529  54 TDYQAALDSAEAQLAKAQAQVARLQAELD----RLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  128 K-RATI--MSLEDF-EQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQ-------------DKPR 190
Cdd:pfam00529 130 RvLAPIggISRESLvTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQiaeaeaelklaklDLER 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 166197652  191 TPM--PGSGQAKRTDMAVQATGSVPSTPVAHRGPSSGLNTPGMFRR 234
Cdd:pfam00529 210 TEIraPVDGTVAFLSVTVDGGTVSAGLRLMFVVPEDNLLVPGMFVE 255
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 26-172 8.32e-04

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: 41.16  E-value: 8.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   26 KQRAENTQEELREFQEGSREYE---AELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEMQHSE--GYR--------Q 92
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNkiiSQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEnqSYKqeiknlesQ 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   93 ISALEDDLAQTKAIKDQLQKYIRELEQANDDLERakraTIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDE 172
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK----EIERLKETIIKNNSEIKD---LTNQDSVKELIIKNLDNTRES 465
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-197 9.44e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 9.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   48 AELEAQLQQIETRNRDLLSENNRLRMELESVKEKFE-MQHSEGY-----------RQISALE----------DDLAQTKA 105
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREaLQRLAEYswdeidvasaeREIAELEaelerldassDDLAALEE 692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIER--------NAFLESELDEK--------------ENLL 163
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaedlaRLELRALLEERfaaalgdaverelrENLE 772

                         170       180       190
                  ....*....|....*....|....*....|....
gi 166197652  164 ESVQRLKDEARDLRQELAVQQKQDKPRTPMPGSG 197
Cdd:COG4913   773 ERIDALRARLNRAEEELERAMRAFNREWPAETAD 806
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 26-171 9.71e-04

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: 40.29  E-value: 9.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  26 KQRAENTQEELREFQEGSREYEAELEAQLQQIEtRNRDLLSE--NNRlrmELESVKEKFEMQHsegyRQISALEDDLAQT 103
Cdd:COG1579   44 EARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNvrNNK---EYEALQKEIESLK----RRISDLEDEILEL 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166197652 104 KAIKDQLQKYIRE----LEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDekENLLESVQRLKD 171
Cdd:COG1579  116 MERIEELEEELAEleaeLAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP--PELLALYERIRK 185
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 28-174 1.03e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.65  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   28 RAENTQEELREFQEGSREYEAELEAQLQQIEtrnrdllsennRLRMELESVKEKFEMQHSEGYRQISALEDDLAQTKAIK 107
Cdd:pfam07888  28 RAELLQNRLEECLQERAELLQAQEAANRQRE-----------KEKERYKRDREQWERQRRELESRVAELKEELRQSREKH 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166197652  108 DQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLEsvqRLKDEAR 174
Cdd:pfam07888  97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE---RMKERAK 160
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 25-180 1.27e-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: 40.77  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   25 YKQRAENTQEELREFQEGSREYEAELEAQLQQIETRN---RDLLSENNRLRMELESVKEKFEMQHsegyRQISALEDdla 101
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNseiKDLTNQDSVKELIIKNLDNTRESLE----TQLKVLSR--- 475

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  102 QTKAIKDQLQKYIRELEQANDDLERAKRATIMS---LEDFEQRLNQAIERNAFLESELDEKENLLESvqrLKDEARDLRQ 178
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELeekVKDLTKKISSLKEKIEKLESEKKEKESKISD---LEDELNKDDF 552


                  ..
gi 166197652  179 EL 180
Cdd:TIGR04523 553 EL 554
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
26-174 1.50e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  26 KQRAENTQE-----ELREFQEGSREYEAELE------AQLQQIETRNRDLLSENNRLRMELEsvkEKFEMQHSEGYRQis 94
Cdd:PRK02224 579 SKLAELKERiesleRIRTLLAAIADAEDEIErlrekrEALAELNDERRERLAEKRERKRELE---AEFDEARIEEARE-- 653

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  95 aledDLAQTKAIKDQLQKYIRELEQANDDLER---AKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKD 171
Cdd:PRK02224 654 ----DKERAEEYLEQVEEKLDELREERDDLQAeigAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRA 729


                 ...
gi 166197652 172 EAR 174
Cdd:PRK02224 730 ELR 732
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
27-181 1.63e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.06  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  27 QRAENTQEELREFQEGSREYEAE---LEAQLQQIETRNrdlLSENnrlrmELESVKEKFE-MQHSEGYRQ-----ISALE 97
Cdd:COG0497  165 RAWRALKKELEELRADEAERAREldlLRFQLEELEAAA---LQPG-----EEEELEEERRrLSNAEKLREalqeaLEALS 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  98 DD----LAQTKAIKDQLQKYIRELEQANDDLERAKRATImSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLK--- 170
Cdd:COG0497  237 GGeggaLDLLGQALRALERLAEYDPSLAELAERLESALI-ELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLArky 315

                        170
                 ....*....|....*
gi 166197652 171 ----DEARDLRQELA 181
Cdd:COG0497  316 gvtvEELLAYAEELR 330
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
25-181 1.64e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  25 YKQRAENTQEELREFQEGSREYE-------------AELEAQLQQIETRNRDLLSENNRLRMELESV-KEKFEMQH---- 86
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEkfikrtenieeliKEKEKELEEVLREINEISSELPELREELEKLeKEVKELEElkee 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  87 -SEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLE-RAKRatimsLEDFEQRLNQAIERNAFLESELDEKENLLE 164
Cdd:PRK03918 240 iEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEeKVKE-----LKELKEKAEEYIKLSEFYEEYLDELREIEK 314

                        170
                 ....*....|....*..
gi 166197652 165 SVQRLKDEARDLRQELA 181
Cdd:PRK03918 315 RLSRLEEEINGIEERIK 331
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 53-186 1.68e-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: 39.52  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  53 QLQQIETRNRDLLSENNRLRMELESVKEKFEmqhsegyrqisALEDDLAQTKAIKDQLQKYIRELEQANDDLE-RAKRA- 130
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELA-----------ALEARLEAAKTELEDLEKEIKRLELEIEEVEaRIKKYe 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166197652 131 ----TIMS---LEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ 186
Cdd:COG1579   80 eqlgNVRNnkeYEALQKEIESLKRRISDLEDEIlelmERIEELEEELAELEAELAELEAELEEKKAE 146
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
34-192 1.83e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  34 EELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEkFEMQHSEGYRQISALEDDLAQTKAIKDQLQKY 113
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE-LEERIEELKKEIEELEEKVKELKELKEKAEEY 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652 114 IReLEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLES-------------ELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:PRK03918 296 IK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeerleelkkklkELEKRLEELEERHELYEEAKAKKEEL 374

                        170
                 ....*....|..
gi 166197652 181 AVQQKQDKPRTP 192
Cdd:PRK03918 375 ERLKKRLTGLTP 386
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 44-79 2.53e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 39.43  E-value: 2.53e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 166197652  44 REYEAELEAQLQQIETRNRDLLSENNRLRMELESVK 79
Cdd:PRK03992   7 EERNSELEEQIRQLELKLRDLEAENEKLERELERLK 42
PilN COG3166
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
138-193 2.54e-03

Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];


Pssm-ID: 442399 [Multi-domain]  Cd Length: 185  Bit Score: 38.41  E-value: 2.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 166197652 138 FEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQDKPRTPM 193
Cdd:COG3166   43 LQGQIAQQQARNAALQQEIAKLDKQIAEIKELKKQKAELLARLQVIEQLQQSRPPW 98
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 3-179 2.59e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 39.56  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   3 DSGKTFESEEEETNYWRDLAMTYKQRaENTQEELREFQEGSRE------YEAELEAQLQQIETRNRDLLSENNRLRMELE 76
Cdd:COG5185  203 TVNSIKESETGNLGSESTLLEKAKEI-INIEEALKGFQDPESEledlaqTSDKLEKLVEQNTDLRLEKLGENAESSKRLN 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  77 SVKEKFEMQHSEGYRQISALEDDLAQTKAIkDQLQKYIRELEqANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESEL 156
Cdd:COG5185  282 ENANNLIKQFENTKEKIAEYTKSIDIKKAT-ESLEEQLAAAE-AEQELEESKRETETGIQNLTAEIEQGQESLTENLEAI 359

                        170       180
                 ....*....|....*....|...
gi 166197652 157 DEKENLLESVQRLKDEARDLRQE 179
Cdd:COG5185  360 KEEIENIVGEVELSKSSEELDSF 382
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
8-174 2.74e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   8 FESEEEETNYWRDLAMTYKQ--RAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLlsenNRLRMELESVKEKF-EM 84
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL----EELRKELEELEKKYsEE 659

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  85 QHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRAtimsledfeqrLNQAIERNAFLESELDEKENLLE 164
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE-----------REKAKKELEKLEKALERVEELRE 728

                        170
                 ....*....|
gi 166197652 165 SVQRLKDEAR 174
Cdd:PRK03918 729 KVKKYKALLK 738
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 25-121 2.76e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.55  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   25 YKQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDL-------LSENNRLRMELESVKEKFE--------MQHS-E 88
Cdd:COG3096   558 LLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELaarapawLAAQDALERLREQSGEALAdsqevtaaMQQLlE 637

                          90       100       110
                  ....*....|....*....|....*....|...
gi 166197652   89 GYRQISALEDDLAQTKAikdQLQKYIRELEQAN 121
Cdd:COG3096   638 REREATVERDELAARKQ---ALESQIERLSQPG 667
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
24-186 3.06e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  24 TYKQRAENTQEELREFQEGSREYEAELEAQLQQIEtrNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISALED----- 98
Cdd:PRK02224 166 EYRERASDARLGVERVLSDQRGSLDQLKAQIEEKE--EKDLHERLNGLESELAELDEEIERYEEQREQARETRDEadevl 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  99 --------DLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLK 170
Cdd:PRK02224 244 eeheerreELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRD 323

                        170
                 ....*....|....*.
gi 166197652 171 DEARDLRQELAVQQKQ 186
Cdd:PRK02224 324 EELRDRLEECRVAAQA 339
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
 142-187 3.19e-03

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 38.81  E-value: 3.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 166197652 142 LNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQD 187
Cdd:PRK13922  71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNLKESLD 116
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
27-190 3.51e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  27 QRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEmqhsegyrQISALEDDLAQTKAI 106
Cdd:COG4372   38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA--------ELAQAQEELESLQEE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652 107 KDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQR--LKDEARDLRQELAVQQ 184
Cdd:COG4372  110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelQALSEAEAEQALDELL 189


                 ....*.
gi 166197652 185 KQDKPR 190
Cdd:COG4372  190 KEANRN 195
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 26-171 3.61e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.17  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   26 KQRAENTQEELREFQEGSREYEAELEA-------------QLQQIETRNRDLLSENNRLRMELESVKEKFEmQHSEGYRQ 92
Cdd:COG3096   305 QYRLVEMARELEELSARESDLEQDYQAasdhlnlvqtalrQQEKIERYQEDLEELTERLEEQEEVVEEAAE-QLAEAEAR 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   93 ISALEDDLaqtKAIKDQLQKYIRELE----------QANDDLERAKR---ATIMSLEDFEQRLNQAIERnaflESELDEK 159
Cdd:COG3096   384 LEAAEEEV---DSLKSQLADYQQALDvqqtraiqyqQAVQALEKARAlcgLPDLTPENAEDYLAAFRAK----EQQATEE 456

                         170
                  ....*....|..
gi 166197652  160 enLLESVQRLKD 171
Cdd:COG3096   457 --VLELEQKLSV 466
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 54-252 3.74e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  54 LQQIETRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIM 133
Cdd:COG3883  124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652 134 SLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQDKPRTPMPGSGQAKRTDMAVQATGSVP 213
Cdd:COG3883  204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAG 283

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 166197652 214 STPVAHRGPSSGLNTPGMFRRGLDSSTSGTPLTPAARIS 252
Cdd:COG3883  284 GGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAV 322
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
91-186 3.90e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   91 RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLN--QAIERNAFLESELDEKENLLESVQR 168
Cdd:COG4913   610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLDASSDDLAA 689

                          90
                  ....*....|....*...
gi 166197652  169 LKDEARDLRQELAVQQKQ 186
Cdd:COG4913   690 LEEQLEELEAELEELEEE 707
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 44-186 5.52e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 38.66  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  44 REYEA--ELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEMQHSEgyrqisaleddLAQTKAIKDQLQKYIRELEQAN 121
Cdd:PRK04778 300 REVKArkYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESE-----------LESVRQLEKQLESLEKQYDEIT 368

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166197652 122 DDLERAKRATIMSLEDFEQRLNQ--AIErnafleselDEKENLLESVQRLKDEARDLRQELAVQQKQ 186
Cdd:PRK04778 369 ERIAEQEIAYSELQEELEEILKQleEIE---------KEQEKLSEMLQGLRKDELEAREKLERYRNK 426
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 20-202 5.61e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 38.55  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   20 DLAMTYKQRAENTQEELR----EFQEGSREYE----------AELEaQLQQIETRNRDLLSENNRLRMELESVKEK---- 81
Cdd:pfam05483 363 ELLRTEQQRLEKNEDQLKiitmELQKKSSELEemtkfknnkeVELE-ELKKILAEDEKLLDEKKQFEKIAEELKGKeqel 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   82 -FEMQHSEgyRQISALEddlAQTKAIKDQLQKYIRELEQANDDLERAKRATI--------MSLEDFE------------Q 140
Cdd:pfam05483 442 iFLLQARE--KEIHDLE---IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIeltahcdkLLLENKEltqeasdmtlelK 516

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166197652  141 RLNQAIERNAFLESE-LDEKENLLESVQRLKDEARDLRQELavQQKQDKPRTPMPGSGQAKRT 202
Cdd:pfam05483 517 KHQEDIINCKKQEERmLKQIENLEEKEMNLRDELESVREEF--IQKGDEVKCKLDKSEENARS 577
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
26-181 5.77e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 5.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   26 KQRAENTQEELREFQEGSREYEAELEA---QLQQIETRNRDLLSENNRLRMELESVKEKFE-MQHSEGYRQISALEDDLA 101
Cdd:COG4913   677 LERLDASSDDLAALEEQLEELEAELEEleeELDELKGEIGRLEKELEQAEEELDELQDRLEaAEDLARLELRALLEERFA 756

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  102 Q----------TKAIKDQLQKYIRELEQANDDLERAKR--------------ATIMSLEDFEQRLNQAIE---------- 147
Cdd:COG4913   757 AalgdaverelRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldADLESLPEYLALLDRLEEdglpeyeerf 836

                         170       180       190
                  ....*....|....*....|....*....|....
gi 166197652  148 RNAFLESELDEKENLLesvQRLKDEARDLRQELA 181
Cdd:COG4913   837 KELLNENSIEFVADLL---SKLRRAIREIKERID 867
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 30-185 6.80e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 38.55  E-value: 6.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   30 ENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVkeKFEMQHSEGYRQisALEDDLAQTKAIKDQ 109
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDI--KMSLQRSMSTQK--ALEEDLQIATKTICQ 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  110 LQKyirELEQANDDLERAK----------RATIMSLEDF----EQRLNQAIERNAFLESELDEKENLLESVQRLKD---- 171
Cdd:pfam05483 329 LTE---EKEAQMEELNKAKaahsfvvtefEATTCSLEELlrteQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNnkev 405

                         170
                  ....*....|....
gi 166197652  172 EARDLRQELAVQQK 185
Cdd:pfam05483 406 ELEELKKILAEDEK 419
mukB PRK04863
chromosome partition protein MukB;
1-186 7.15e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.40  E-value: 7.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    1 MEDSGKTFESEEEETNYWRDLAMTykqrAENTQEELREFQEGSREYEAELEAQL--------QQIETRNRDLLSEN--NR 70
Cdd:PRK04863  319 LNEAESDLEQDYQAASDHLNLVQT----ALRQQEKIERYQADLEELEERLEEQNevveeadeQQEENEARAEAAEEevDE 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   71 LRMELESVKEKFEMQHSEG--YRQ-ISALE--------DDLAQTKAIK--DQLQKYIRELEQANDDLERAKRATIMSLED 137
Cdd:PRK04863  395 LKSQLADYQQALDVQQTRAiqYQQaVQALErakqlcglPDLTADNAEDwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQ 474

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166197652  138 FEQ------RLNQAIERNAF------LESELDEKENLLESVQRLKDEARDLRQELAVQQKQ 186
Cdd:PRK04863  475 FEQayqlvrKIAGEVSRSEAwdvareLLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA 535
fliH PRK06669
flagellar assembly protein H; Validated
 67-180 7.39e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 37.69  E-value: 7.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  67 ENNRLRMELESVKEKFEMQHSEGYRQIS--ALEDDLAQTKAIKDQLqkyIRELEQANDDLERAKRATIMSLE----DFEQ 140
Cdd:PRK06669  34 EKERLREEEEEQVEQLREEANDEAKEIIeeAEEDAFEIVEAAEEEA---KEELLKKTDEASSIIEKLQMQIEreqeEWEE 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 166197652 141 RLNQAIER---NAFLESELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:PRK06669 111 ELERLIEEakaEGYEEGYEKGREEGLEEVRELIEQLNKIIEKL 153
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 45-181 8.76e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 38.23  E-value: 8.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652    45 EYEAELEAQLQQIETRNRDLLSENNRLRMELE----------SVKEKFEMQHSEGYRQISAL----EDDLAQTKAIKDQL 110
Cdd:pfam01576  728 QFERDLQARDEQGEEKRRQLVKQVRELEAELEderkqraqavAAKKKLELDLKELEAQIDAAnkgrEEAVKQLKKLQAQM 807

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166197652   111 QKYIRELEQAnddleRAKRATIMSL-EDFEQRLNQaiernafLESELDEKENLLESVQRLKDEARDLRQELA 181
Cdd:pfam01576  808 KDLQRELEEA-----RASRDEILAQsKESEKKLKN-------LEAELLQLQEDLAASERARRQAQQERDELA 867
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 55-186 8.82e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 37.80  E-value: 8.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   55 QQIETRNRDLLSENNRLRMELESVKEKFEMQhsegyRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIms 134
Cdd:pfam05557   3 ELIESKARLSQLQNEKKQMELEHKRARIELE-----KKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQA-- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 166197652  135 leDFEQRLNQAIERNAFLESELDEKENLLESVQR-LKDEARDLRQELAVQQKQ 186
Cdd:pfam05557  76 --ELNRLKKKYLEALNKKLNEKESQLADAREVIScLKNELSELRRQIQRAELE 126
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 107-338 8.89e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 38.10  E-value: 8.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  107 KDQLQKYIRELEQANDDLERAKRATI--MSLEDfeqrLNQAIErnaFLESELDEKENLLESVQRLKDEARDLRQELAVQQ 184
Cdd:PTZ00108 1101 KEKVEKLNAELEKKEKELEKLKNTTPkdMWLED----LDKFEE---ALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPK 1173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  185 KQDKPRtpmpgSGQAKRTDMAVQATGSVPSTPVAHRGPSSGLNTPGMFRRGLDSSTSGTPLTPAARISALNIVGDLLRKV 264
Cdd:PTZ00108 1174 LKKKEK-----KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKN 1248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  265 GALESKLASCRNFMYD--------------QSPSRTSGPASGRGTKNRDGVDRRPGSTSVGDKGSGKRLEFGKPASEPAS 330
Cdd:PTZ00108 1249 NSSKSSEDNDEFSSDDlskegkpknapkrvSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSE 1328


                  ....*...
gi 166197652  331 PALPSAQG 338
Cdd:PTZ00108 1329 KKTARKKK 1336
GrpE pfam01025
GrpE;
47-127 9.06e-03

GrpE;


Pssm-ID: 425996 [Multi-domain]  Cd Length: 165  Bit Score: 36.43  E-value: 9.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652   47 EAELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEmqhsegyRQISaleddlaqtKAIKDQLQKYIRELEQANDDLER 126
Cdd:pfam01025  13 IESLEEEIEELEKKIEELKEKLLRALAEFENLRKRTE-------KEKE---------EAKKFAIEKFAKDLLPVIDNLER 76


                  .
gi 166197652  127 A 127
Cdd:pfam01025  77 A 77
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
26-186 9.97e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 37.69  E-value: 9.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652  26 KQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESvkeKFEMQhsegyrQISALEDDLAQTKA 105
Cdd:COG3206  163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEA---KLLLQ------QLSELESQLAEARA 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197652 106 IKDQLQKYIRELEQANDDLERAKRATIMSledfeQRLNQAIERNAFLESELDEKENLL----ESVQRLKDEARDLRQELA 181
Cdd:COG3206  234 ELAEAEARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYtpnhPDVIALRAQIAALRAQLQ 308


                 ....*
gi 166197652 182 VQQKQ 186
Cdd:COG3206  309 QEAQR 313
 
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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