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Conserved domains on  [gi|1034594996|ref|XP_016878842|]
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nuclear distribution protein nudE homolog 1 isoform X6 [Homo sapiens]

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 1.01e-53

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: 173.44  E-value: 1.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 134 SLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ------EKPRTPMPSSVEAERTD 203
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKlrnllmRSPSTPSLQTLEIFDRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 204 TAVQATgsvpSTPIAHRGPSSSLNtpgSFRRGlddSTGGTPLTPAARISAlnivgDLLRKVGALESKLASCRNLVYDQSP 283
Cdd:pfam04880  81 PAVQAV----SSPVIATPPEKSFN---SLRTG---SETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNA 145

                         170       180
                  ....*....|....*....|....*.
gi 1034594996 284 NRtggpasgRSSKNRDGGERRPSSTS 309
Cdd:pfam04880 146 SR-------RGNSRSLYGSRPPTKFA 164
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-187 5.30e-08

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 5.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  27 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEV---QHSEGYRQISALEDDLAQT 103
Cdd:COG1196   270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEleeELEELEEELEELEEELEEA 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 104 KAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQ 183
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429


                  ....
gi 1034594996 184 QKQE 187
Cdd:COG1196   430 LAEL 433
 
Name Accession Description Interval E-value
NUDE_C pfam04880
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ...
 134-309 1.01e-53

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: 173.44  E-value: 1.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 134 SLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ------EKPRTPMPSSVEAERTD 203
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKlrnllmRSPSTPSLQTLEIFDRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 204 TAVQATgsvpSTPIAHRGPSSSLNtpgSFRRGlddSTGGTPLTPAARISAlnivgDLLRKVGALESKLASCRNLVYDQSP 283
Cdd:pfam04880  81 PAVQAV----SSPVIATPPEKSFN---SLRTG---SETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNA 145

                         170       180
                  ....*....|....*....|....*.
gi 1034594996 284 NRtggpasgRSSKNRDGGERRPSSTS 309
Cdd:pfam04880 146 SR-------RGNSRSLYGSRPPTKFA 164
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-187 5.30e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 5.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  27 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEV---QHSEGYRQISALEDDLAQT 103
Cdd:COG1196   270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEleeELEELEEELEELEEELEEA 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 104 KAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQ 183
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429


                  ....
gi 1034594996 184 QKQE 187
Cdd:COG1196   430 LAEL 433
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-186 7.75e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 7.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   26 KQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  106 -------IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168  818 eaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897


                   ....*...
gi 1034594996  179 ELAVQQKQ 186
Cdd:TIGR02168  898 ELSEELRE 905
mukB PRK04863
chromosome partition protein MukB;
41-186 4.40e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 48.41  E-value: 4.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   41 EGSREYEAELETQLQQIETRnrdLLSENNRLRMElETIKEKFE------------VQHSEGYRQISALEDDLAQTKAIKD 108
Cdd:PRK04863   438 DNAEDWLEEFQAKEQEATEE---LLSLEQKLSVA-QAAHSQFEqayqlvrkiageVSRSEAWDVARELLRRLREQRHLAE 513

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  109 QLQKY---IRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:PRK04863   514 QLQQLrmrLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLE 589


                   .
gi 1034594996  186 Q 186
Cdd:PRK04863   590 Q 590
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 26-253 1.63e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGyrqISALEDDLAQTKA 105
Cdd:COG3883    50 NEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGSES---FSDFLDRLSALSK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG3883   127 IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034594996 186 QEKPRTPMPSSVEAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGSFRRGLDDSTGGTPLTPAARISA 253
Cdd:COG3883   207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 19-147 2.87e-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: 45.05  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  19 KDLAMTYKQRAENTQEELREFQEGSREYeaelETQLQQIETRNRDLLSENNRL--RMELETIKEkfevqhsegyrQISAL 96
Cdd:cd22656   127 LKEAKKYQDKAAKVVDKLTDFENQTEKD----QTALETLEKALKDLLTDEGGAiaRKEIKDLQK-----------ELEKL 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034594996  97 EDDLAqtKAIKDQLQKYIRELEQANDDLERAKR------ATIMSLEDFEQRLNQAIE 147
Cdd:cd22656   192 NEEYA--AKLKAKIDELKALIADDEAKLAAALRliadltAADTDLDNLLALIGPAIP 246
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 20-190 2.74e-04

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: 42.52  E-value: 2.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   20 DLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSE------GYRQ- 92
Cdd:pfam12128  643 FARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREartekqAYWQv 722

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   93 -ISALEDDLAQTKAIKDQLQ------------KYIREL------EQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLE 153
Cdd:pfam12128  723 vEGALDAQLALLKAAIAARRsgakaelkaletWYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQ 802

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1034594996  154 SE-LDEKENLLESVQRLKDEARDLRQELAVQQKQEKPR 190
Cdd:pfam12128  803 ETwLQRRPRLATQLSNIERAISELQQQLARLIADTKLR 840
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
 142-204 1.55e-03

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 39.58  E-value: 1.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034594996 142 LNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVqqKQEKPRTPMPSSVEAERTDT 204
Cdd:PRK13922   71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNL--KESLDYQFITARVISRSPDP 131
 
Name Accession Description Interval E-value
NUDE_C pfam04880
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ...
 134-309 1.01e-53

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: 173.44  E-value: 1.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 134 SLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ------EKPRTPMPSSVEAERTD 203
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKlrnllmRSPSTPSLQTLEIFDRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 204 TAVQATgsvpSTPIAHRGPSSSLNtpgSFRRGlddSTGGTPLTPAARISAlnivgDLLRKVGALESKLASCRNLVYDQSP 283
Cdd:pfam04880  81 PAVQAV----SSPVIATPPEKSFN---SLRTG---SETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNA 145

                         170       180
                  ....*....|....*....|....*.
gi 1034594996 284 NRtggpasgRSSKNRDGGERRPSSTS 309
Cdd:pfam04880 146 SR-------RGNSRSLYGSRPPTKFA 164
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-187 5.30e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 5.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  27 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEV---QHSEGYRQISALEDDLAQT 103
Cdd:COG1196   270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEleeELEELEEELEELEEELEEA 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 104 KAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQ 183
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429


                  ....
gi 1034594996 184 QKQE 187
Cdd:COG1196   430 LAEL 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-188 6.80e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 6.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  26 KQRAENTQEELREFQEGSREYEAELEtQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196   273 RLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQ----RLKDEARDLRQELA 181
Cdd:COG1196   352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLerleRLEEELEELEEALA 431


                  ....*..
gi 1034594996 182 VQQKQEK 188
Cdd:COG1196   432 ELEEEEE 438
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 11-188 7.30e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 7.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  11 EEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGY 90
Cdd:COG1196   300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  91 RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLK 170
Cdd:COG1196   380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                         170
                  ....*....|....*...
gi 1034594996 171 DEARDLRQELAVQQKQEK 188
Cdd:COG1196   460 ALLELLAELLEEAALLEA 477
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-186 7.75e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 7.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   26 KQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  106 -------IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168  818 eaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897


                   ....*...
gi 1034594996  179 ELAVQQKQ 186
Cdd:TIGR02168  898 ELSEELRE 905
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-187 9.29e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 9.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196   318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196   398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477


                  ..
gi 1034594996 186 QE 187
Cdd:COG1196   478 AL 479
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 24-188 2.35e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  24 TYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRM------ELETIKEKFEVQHSEGYRQISALE 97
Cdd:COG1196   243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaelaRLEQDIARLEERRRELEERLEELE 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  98 DDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLR 177
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE---LAEAEEELEELAEELLEALRAAAELA 399

                         170
                  ....*....|.
gi 1034594996 178 QELAVQQKQEK 188
Cdd:COG1196   400 AQLEELEEAEE 410
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-187 2.35e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHsegyRQISALEDDLAQTKA 105
Cdd:COG1196   329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL----EALRAAAELAAQLEE 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196   405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484


                  ..
gi 1034594996 186 QE 187
Cdd:COG1196   485 EL 486
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
27-201 6.01e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 6.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   27 QRAENTQEELREFQEGSREYEAE-----LETQLQQIETRNRDLLSENNRLRMELETIKEK---FEVQHSE-GYRQISALE 97
Cdd:COG4913    265 AAARERLAELEYLRAALRLWFAQrrlelLEAELEELRAELARLEAELERLEARLDALREEldeLEAQIRGnGGDRLEQLE 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   98 DDLAQTKAIKDQLQkyiRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEN----LLESVQRLKDEA 173
Cdd:COG4913    345 REIERLERELEERE---RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRREL 421

                          170       180
                   ....*....|....*....|....*...
gi 1034594996  174 RDLRQELAVQQKQekpRTPMPSSVEAER 201
Cdd:COG4913    422 RELEAEIASLERR---KSNIPARLLALR 446
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-200 6.45e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 6.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   48 AELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVqhSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERA 127
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREA--LQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAAL 690

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034594996  128 KR---ATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSSVEAE 200
Cdd:COG4913    691 EEqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 34-186 7.60e-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: 50.83  E-value: 7.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   34 EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYR---QISALEDDLAQTKAIKDQL 110
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARleaEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034594996  111 QKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEARDLRQELAVQQKQ 186
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR---AELTLLNEEAANLRERLESLERR 832
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-188 1.54e-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: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEvqhsegyrqisALEDDLAQTKA 105
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE-----------EAEAELAEAEE 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196   366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA---EEALLERLERLEEELEELEEALAELEEEEEEEEE 442


                  ...
gi 1034594996 186 QEK 188
Cdd:COG1196   443 ALE 445
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 26-211 2.08e-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: 48.61  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  26 KQRAENTQEELREFQEGSREYEA---ELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQ---------- 92
Cdd:COG4942    47 KKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalll 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  93 ----ISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLesvQR 168
Cdd:COG4942   127 spedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL---AR 203

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034594996 169 LKDEARDLRQELAVQQKQEKPRTPMPSSVEAERTDTAVQATGS 211
Cdd:COG4942   204 LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
27-186 3.28e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  27 QRAENTQEELREFQEGSREYeAELETQLQQIETRNRDLLSENNRLRMELETIKEkfEVQHSEGYRQISALEDDLAQTKAI 106
Cdd:COG4717    71 KELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEKLEK--LLQLLPLYQELEALEAELAELPER 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 107 KDQLQKYIRELEQANDDLERAKRAtimsLEDFEQRLNQAIERnaFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQ 186
Cdd:COG4717   148 LEELEERLEELRELEEELEELEAE----LAELQEELEELLEQ--LSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-181 3.77e-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: 48.51  E-value: 3.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   26 KQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIE-ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL------------ESVQRLKDEA 173
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaealenkieDDEEEARRRL 974


                   ....*...
gi 1034594996  174 RDLRQELA 181
Cdd:TIGR02168  975 KRLENKIK 982
mukB PRK04863
chromosome partition protein MukB;
41-186 4.40e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 48.41  E-value: 4.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   41 EGSREYEAELETQLQQIETRnrdLLSENNRLRMElETIKEKFE------------VQHSEGYRQISALEDDLAQTKAIKD 108
Cdd:PRK04863   438 DNAEDWLEEFQAKEQEATEE---LLSLEQKLSVA-QAAHSQFEqayqlvrkiageVSRSEAWDVARELLRRLREQRHLAE 513

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  109 QLQKY---IRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:PRK04863   514 QLQQLrmrLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLE 589


                   .
gi 1034594996  186 Q 186
Cdd:PRK04863   590 Q 590
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
24-186 4.81e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.09  E-value: 4.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  24 TYKQRAENTQEELREFQEGSREYE------------AELETQLQQIETRNRDLLSENNRLRMELETIKEkfEVQHSEGYR 91
Cdd:COG3206   186 ELRKELEEAEAALEEFRQKNGLVDlseeaklllqqlSELESQLAEARAELAEAEARLAALRAQLGSGPD--ALPELLQSP 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  92 QISALEDDLAQTKA-IKDQLQKY------IRELEQANDDLERAKRATI-MSLEDFEQRLNQAIERNAFLESELDEKENLL 163
Cdd:COG3206   264 VIQQLRAQLAELEAeLAELSARYtpnhpdVIALRAQIAALRAQLQQEAqRILASLEAELEALQAREASLQAQLAQLEARL 343

                         170       180
                  ....*....|....*....|...
gi 1034594996 164 ESVQRLKDEARDLRQELAVQQKQ 186
Cdd:COG3206   344 AELPELEAELRRLEREVEVAREL 366
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 19-181 4.87e-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: 4.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   19 KDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSegyrQISALED 98
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN----EIERLEA 407

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   99 DLAQTKAIKDQLQKYIRELEQANDDLEraKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168  408 RLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485


                   ...
gi 1034594996  179 ELA 181
Cdd:TIGR02168  486 QLQ 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-187 5.18e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 5.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRnrdlLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE----LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196   422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501


                  ..
gi 1034594996 186 QE 187
Cdd:COG1196   502 DY 503
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 30-188 6.94e-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: 47.71  E-value: 6.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  30 ENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRL---RMELETIK-EKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLnqlKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQN 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 106 IKDQLQKYIRELEQANDDLERakraTIMSLEDFEQRLNQAI-ERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQ 184
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKK----ELTNSESENSEKQRELeEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404


                  ....
gi 1034594996 185 KQEK 188
Cdd:TIGR04523 405 KLNQ 408
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-180 7.71e-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: 47.74  E-value: 7.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   27 QRAENTQEELREFQEGS-----REYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKfEVQHSEGYRQISALEDDLA 101
Cdd:TIGR02168  213 ERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELEEEIEELQKELY 291

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034594996  102 QTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 11-173 1.21e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   11 EEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEA-----------------ELETQLQQIETRNRDLLSENNRLRM 73
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAalrdlesrlgdlkkerdELEAQLRELERKIEELEAQIEKKRK 917

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   74 ELETIKEKFEVQHSEgyrqISALEDDLAQTKAIK------DQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIE 147
Cdd:TIGR02169  918 RLSELKAKLEALEEE----LSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993

                          170       180
                   ....*....|....*....|....*.
gi 1034594996  148 RNAFLESELDEKENLLESVQRLKDEA 173
Cdd:TIGR02169  994 KRAKLEEERKAILERIEEYEKKKREV 1019
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 48-188 1.35e-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: 45.69  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  48 AELETQLQQIETRNRDLLSENNRLRMELETIK---EKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYI------RELE 118
Cdd:COG1579    13 QELDSELDRLEHRLKELPAELAELEDELAALEarlEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnKEYE 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034594996 119 QANDDLERAKRAtIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQ-RLKDEARDLRQELAVQQKQEK 188
Cdd:COG1579    93 ALQKEIESLKRR-ISDLEDEILELMERIEE---LEEELAELEAELAELEaELEEKKAELDEELAELEAELE 159
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 26-253 1.63e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGyrqISALEDDLAQTKA 105
Cdd:COG3883    50 NEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGSES---FSDFLDRLSALSK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG3883   127 IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034594996 186 QEKPRTPMPSSVEAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGSFRRGLDDSTGGTPLTPAARISA 253
Cdd:COG3883   207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-191 2.00e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996    1 MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEA---ELETQLQQIETRNRDLLSENNRLRMELET 77
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESkrsELRRELEELREKLAQLELRLEGLEVRIDN 940

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   78 IKEKFEVQHSegyrqiSALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEqrlnQAIERNAFLESELD 157
Cdd:TIGR02168  941 LQERLSEEYS------LTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYE----ELKERYDFLTAQKE 1010

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1034594996  158 E----KENLLESVQRLKDEARDLRQELAVQQKQEKPRT 191
Cdd:TIGR02168 1011 DlteaKETLEEAIEEIDREARERFKDTFDQVNENFQRV 1048
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1-188 2.05e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996    1 MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLlsenNRLRMELETIK- 79
Cdd:TIGR02169  711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEa 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   80 --------------EKFEVQHSEGYRQISALEDDLAQTKAIKDQLQK-------YIRELE-------QANDDLERAKRAT 131
Cdd:TIGR02169  787 rlshsripeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKeiqelqeQRIDLKeqiksieKEIENLNGKKEEL 866

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034594996  132 IMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 188
Cdd:TIGR02169  867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-196 2.40e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 2.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   48 AELETQLQQIETRNRDLLSENNRLRmELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQkyiRELEQANDDLERA 127
Cdd:COG4913    664 ASAEREIAELEAELERLDASSDDLA-ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE---EELDELQDRLEAA 739

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  128 -KRATIMSLEDFEQRLNQAIERNAflesELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSS 196
Cdd:COG4913    740 eDLARLELRALLEERFAAALGDAV----ERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETA 805
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-188 2.56e-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: 45.82  E-value: 2.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   25 YKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSEN---NRLRMELETIKEKFEVQHS---EGYRQISALED 98
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRealDELRAELTLLNEEAANLRErleSLERRIAATER 838

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   99 DLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                          170
                   ....*....|
gi 1034594996  179 ELAVQQKQEK 188
Cdd:TIGR02168  919 ELREKLAQLE 928
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-187 2.84e-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: 45.82  E-value: 2.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   25 YKQRAENTQEELREFQ---EGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKF----------EVQHSEGYR 91
Cdd:TIGR02168  251 AEEELEELTAELQELEeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanlerqleelEAQLEELES 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   92 QISALEDDLAQTKAIKDQLQKYIRELEQAND-------DLERAKRATIMSLEDFEQRLNQAIERNAFLESEL----DEKE 160
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIerleARLE 410

                          170       180
                   ....*....|....*....|....*..
gi 1034594996  161 NLLESVQRLKDEARDLRQELAVQQKQE 187
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLKKLEEAELKE 437
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 19-147 2.87e-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: 45.05  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  19 KDLAMTYKQRAENTQEELREFQEGSREYeaelETQLQQIETRNRDLLSENNRL--RMELETIKEkfevqhsegyrQISAL 96
Cdd:cd22656   127 LKEAKKYQDKAAKVVDKLTDFENQTEKD----QTALETLEKALKDLLTDEGGAiaRKEIKDLQK-----------ELEKL 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034594996  97 EDDLAqtKAIKDQLQKYIRELEQANDDLERAKR------ATIMSLEDFEQRLNQAIE 147
Cdd:cd22656   192 NEEYA--AKLKAKIDELKALIADDEAKLAAALRliadltAADTDLDNLLALIGPAIP 246
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 24-196 3.06e-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: 45.14  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  24 TYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFevqhSEGYRQISALEDDLAQT 103
Cdd:COG4942    73 ALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDF----LDAVRRLQYLKYLAPAR 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 104 KAIKDQLQKYIRELEQANDDLERAK---RATIMSLEDFEQRLNQAIERNAFLESELDEKENLLES-VQRLKDEARDLRQE 179
Cdd:COG4942   149 REQAEELRADLAELAALRAELEAERaelEALLAELEEERAALEALKAERQKLLARLEKELAELAAeLAELQQEAEELEAL 228

                         170
                  ....*....|....*..
gi 1034594996 180 LAVQQKQEKPRTPMPSS 196
Cdd:COG4942   229 IARLEAEAAAAAERTPA 245
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
47-191 3.43e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  47 EAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHsegyRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLER 126
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREELEKLEK 123

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034594996 127 AKRA--TIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRT 191
Cdd:COG4717   124 LLQLlpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 27-181 4.73e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 4.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   27 QRAENTQEELREFQEGSREYEA--------ELETQLQQIETRnrdllsennrlRMELETIKEKFEVQHSEGYRQISALED 98
Cdd:TIGR02169  204 RREREKAERYQALLKEKREYEGyellkekeALERQKEAIERQ-----------LASLEEELEKLTEEISELEKRLEEIEQ 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   99 DLAQ-TKAIKD-------QLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELD-----------EK 159
Cdd:TIGR02169  273 LLEElNKKIKDlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEelereieeerkRR 352

                          170       180
                   ....*....|....*....|..
gi 1034594996  160 ENLLESVQRLKDEARDLRQELA 181
Cdd:TIGR02169  353 DKLTEEYAELKEELEDLRAELE 374
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 95-186 7.73e-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: 43.98  E-value: 7.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  95 ALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEAR 174
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEIA 93

                          90
                  ....*....|..
gi 1034594996 175 DLRQELAVQQKQ 186
Cdd:COG4942    94 ELRAELEAQKEE 105
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 37-187 1.36e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  37 REFQEGSREYEAEL--------ETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYR---QISALEDDLAQTKA 105
Cdd:COG1196   216 RELKEELKELEAELlllklrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEElelELEEAQAEEYELLA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375


                  ..
gi 1034594996 186 QE 187
Cdd:COG1196   376 EA 377
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 10-176 1.96e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   10 SEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELET---QLQQIETRNRDLLSENNRLRMELETIKEKFEVQh 86
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQEIEELLKKLEEA- 433

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   87 segyrQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESV 166
Cdd:TIGR02168  434 -----ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508

                          170
                   ....*....|
gi 1034594996  167 QRLKDEARDL 176
Cdd:TIGR02168  509 KALLKNQSGL 518
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 91-163 2.62e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 2.62e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034594996  91 RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL 163
Cdd:COG4942    34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 20-190 2.74e-04

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: 42.52  E-value: 2.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   20 DLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSE------GYRQ- 92
Cdd:pfam12128  643 FARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREartekqAYWQv 722

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   93 -ISALEDDLAQTKAIKDQLQ------------KYIREL------EQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLE 153
Cdd:pfam12128  723 vEGALDAQLALLKAAIAARRsgakaelkaletWYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQ 802

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1034594996  154 SE-LDEKENLLESVQRLKDEARDLRQELAVQQKQEKPR 190
Cdd:pfam12128  803 ETwLQRRPRLATQLSNIERAISELQQQLARLIADTKLR 840
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 29-187 2.86e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 2.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   29 AENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEK----------FEVQHSEGYRQISALED 98
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlskelteLEAEIEELEERLEEAEE 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   99 DLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855


                   ....*....
gi 1034594996  179 ELAVQQKQE 187
Cdd:TIGR02168  856 SLAAEIEEL 864
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 48-164 3.08e-04

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 41.05  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  48 AELETQLQQIETRNRDLLSENNRLRMELETIKEKFEV--QHSEGYRQISAledDLAQTKAIKDQLQKYIRELEQANDDLE 125
Cdd:pfam13851  36 AELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEElrKQLENYEKDKQ---SLKNLKARLKVLEKELKDLKWEHEVLE 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1034594996 126 RAKRATIMSLEDFEQRLNQAIE--------RNAFLESELDEKENLLE 164
Cdd:pfam13851 113 QRFEKVERERDELYDKFEAAIQdvqqktglKNLLLEKKLQALGETLE 159
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
24-190 5.95e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 5.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  24 TYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRD-----LLSENNRLRMELETIKEKFEVQHSegyrQISALED 98
Cdd:COG3206   223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpviqqLRAQLAELEAELAELSARYTPNHP----DVIALRA 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  99 DLAQTKA-IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIErnafLESELDEKENLLESVQRLKDEARDLR 177
Cdd:COG3206   299 QIAALRAqLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELYESLLQRL 374

                         170
                  ....*....|...
gi 1034594996 178 QELAVQQKQEKPR 190
Cdd:COG3206   375 EEARLAEALTVGN 387
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 19-188 6.63e-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: 41.64  E-value: 6.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   19 KDLAMTYKQRAENTQEEL-REFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALE 97
Cdd:pfam15921  244 EDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLE 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   98 DDLAQtkaIKDQLQKYIRELEQANDDLEraKRATIMSLEDFEQRlnqaIERNAFLEseldEKENLLESVQRLKDEARDLR 177
Cdd:pfam15921  324 STVSQ---LRSELREAKRMYEDKIEELE--KQLVLANSELTEAR----TERDQFSQ----ESGNLDDQLQKLLADLHKRE 390

                          170
                   ....*....|.
gi 1034594996  178 QELAVQQKQEK 188
Cdd:pfam15921  391 KELSLEKEQNK 401
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 40-190 8.43e-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: 41.09  E-value: 8.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   40 QEGSREYEAELETQLQQIETRNRDL-----LSENNRLRME-----LETIKEkfEVQHSEGYRQISALEDDLAQTKAIKDQ 109
Cdd:COG3096    436 PENAEDYLAAFRAKEQQATEEVLELeqklsVADAARRQFEkayelVCKIAG--EVERSQAWQTARELLRRYRSQQALAQR 513

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  110 LQKYIRELEQANDDLERAKRATIMsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKP 189
Cdd:COG3096    514 LQQLRAQLAELEQRLRQQQNAERL-LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592


                   .
gi 1034594996  190 R 190
Cdd:COG3096    593 R 593
PilN COG3166
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
138-193 1.30e-03

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


Pssm-ID: 442399 [Multi-domain]  Cd Length: 185  Bit Score: 39.18  E-value: 1.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034594996 138 FEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPM 193
Cdd:COG3166    43 LQGQIAQQQARNAALQQEIAKLDKQIAEIKELKKQKAELLARLQVIEQLQQSRPPW 98
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-176 1.33e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  27 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAI 106
Cdd:COG1196   682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034594996 107 KDQLQKYIRELEQANDDLE----RAkratimsLEDFEqrlnQAIERNAFLESELD----EKENLLESVQRLKDEARDL 176
Cdd:COG1196   762 LEELERELERLEREIEALGpvnlLA-------IEEYE----ELEERYDFLSEQREdleeARETLEEAIEEIDRETRER 828
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 21-190 1.33e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.49  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  21 LAMTYKQRAENTQEELREFQ-EGSREYEAELE-TQLQQIETRNRDLLSENNRLRMELETIKeKFEVQHSEGYRQISALED 98
Cdd:pfam17380 342 MAMERERELERIRQEERKRElERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAAR-KVKILEEERQRKIQQQKV 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  99 DLAQTKAIKDQL-QKYIRELEQanddlERAKRATIMSLEDFEQRlnQAIERNAFLESELDEKENLLESVQRLKDEARDLR 177
Cdd:pfam17380 421 EMEQIRAEQEEArQREVRRLEE-----ERAREMERVRLEEQERQ--QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR 493

                         170
                  ....*....|...
gi 1034594996 178 QELAVQQKQEKPR 190
Cdd:pfam17380 494 RKILEKELEERKQ 506
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
 142-204 1.55e-03

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 39.58  E-value: 1.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034594996 142 LNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVqqKQEKPRTPMPSSVEAERTDT 204
Cdd:PRK13922   71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNL--KESLDYQFITARVISRSPDP 131
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 44-189 1.69e-03

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: 40.04  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   44 REYEAELETQlqQIETRNRDLLSENNRLRmELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDD 123
Cdd:TIGR02168  216 KELKAELREL--ELALLVLRLEELREELE-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034594996  124 LERAkratimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKP 189
Cdd:TIGR02168  293 LANE-------ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
PRK14160 PRK14160
heat shock protein GrpE; Provisional
 1-188 1.98e-03

heat shock protein GrpE; Provisional


Pssm-ID: 237629 [Multi-domain]  Cd Length: 211  Bit Score: 38.97  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   1 MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREF--QEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETI 78
Cdd:PRK14160    1 MEKECKDAKHENMEEDCCKENENKEEDKGKEEDLEFEEIekEEIIEDSEESNEVKIEELKDENNKLKEENKKLENELEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  79 KEKFE--VQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELeqanDDLERAKrATIMSLEDFEQRLNQAIE--RNAF--- 151
Cdd:PRK14160   81 KDRLLrtVAEYDNYRKRTAKEKEGIYSDACEDVLKELLPVL----DNLERAA-AVEGSVEDLKKGIEMTVKqfKTSLekl 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034594996 152 ----LESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 188
Cdd:PRK14160  156 gveeISTEGEFDPNLHNAVMHVEDENYGENEIVEVFQKGYK 196
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 26-174 2.19e-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: 38.75  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  26 KQRAENTQEELREFQEGSREYEAELETQLQQIEtrnrDLLSENNRLRMELETIK---EKFEVQHSEG--YRQISALEDDL 100
Cdd:COG1579    23 EHRLKELPAELAELEDELAALEARLEAAKTELE----DLEKEIKRLELEIEEVEariKKYEEQLGNVrnNKEYEALQKEI 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034594996 101 AQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEAR 174
Cdd:COG1579    99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELA 169
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 38-79 2.28e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 39.43  E-value: 2.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034594996  38 EFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIK 79
Cdd:PRK03992    1 ERLEALEERNSELEEQIRQLELKLRDLEAENEKLERELERLK 42
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 33-184 2.76e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 2.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   33 QEELREFQEGSREYEAELETQLQQIETRNRDLlsenNRLRMELETIKEKFEvqhsEGYRQISALEDDLAQTKAIKDQLQK 112
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSDASRKIGEIEKEI----EQLEQEEEKLKERLE----ELEEDLSSLEQEIENVKSELKELEA 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  113 YIRELEQANDDLERAkratimsLEDFEQRLNQAI------------ERNAFLESELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:TIGR02169  766 RIEELEEDLHKLEEA-------LNDLEARLSHSRipeiqaelskleEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838


                   ....
gi 1034594996  181 AVQQ 184
Cdd:TIGR02169  839 QEQR 842
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
12-180 3.22e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  12 EEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELEtQLQQIETR------NRDLLSENNRLRMELETIKEKFEVQ 85
Cdd:PRK02224  550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERIRTLlaaiadAEDEIERLREKREALAELNDERRER 628

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  86 HSEGYRQISALEDD-----LAQTKAIKDQLQKYIRELEQANDDLERAK---RATIMSLEDFEQRLNQAIERNAFLESELD 157
Cdd:PRK02224  629 LAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERddlQAEIGAVENELEELEELRERREALENRVE 708

                         170       180
                  ....*....|....*....|...
gi 1034594996 158 EKENLLESVQRLKDEARDLRQEL 180
Cdd:PRK02224  709 ALEALYDEAEELESMYGDLRAEL 731
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 28-174 3.55e-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: 38.72  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  28 RAENTQEELrefqEGSREYEAELetqLQQIETRNRDLLSEnnrlRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIK 107
Cdd:pfam07888  28 RAELLQNRL----EECLQERAEL---LQAQEAANRQREKE----KERYKRDREQWERQRRELESRVAELKEELRQSREKH 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034594996 108 DQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLEsvqRLKDEAR 174
Cdd:pfam07888  97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE---RMKERAK 160
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 19-180 4.31e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 4.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   19 KDLAMTYKQRAEnTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALED 98
Cdd:TIGR02169  237 RQKEAIERQLAS-LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   99 DLAQTKAIKDQLQKYIRELEQANDDLERakratimSLEDFEQRLNQAIERNAFLESELDEKENLLESV----QRLKDEAR 174
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEELER-------EIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefAETRDELK 388


                   ....*.
gi 1034594996  175 DLRQEL 180
Cdd:TIGR02169  389 DYREKL 394
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
28-186 4.45e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 4.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  28 RAENTQEELREFQEGSREYEAELETQLQQIETRnrdlLSENNRLrmeLETIKEKFEVQHSEGYRQISALEDDLAQTKAIK 107
Cdd:PRK02224  409 NAEDFLEELREERDELREREAELEATLRTARER----VEEAEAL---LEAGKCPECGQPVEGSPHVETIEEDRERVEELE 481

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 108 DQLQKYIRELEQANDDLERAKratimSLEDFEQRLNQAIERNAFLESELDEKENLLES----VQRLKDEARDLRQELAVQ 183
Cdd:PRK02224  482 AELEDLEEEVEEVEERLERAE-----DLVEAEDRIERLEERREDLEELIAERRETIEEkrerAEELRERAAELEAEAEEK 556


                  ...
gi 1034594996 184 QKQ 186
Cdd:PRK02224  557 REA 559
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
34-192 4.49e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 4.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  34 EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEkFEVQHSEGYRQISALEDDLAQTKAIKDQLQKY 113
Cdd:PRK03918  217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE-LEERIEELKKEIEELEEKVKELKELKEKAEEY 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 114 IReLEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLES-------------ELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:PRK03918  296 IK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeerleelkkklkELEKRLEELEERHELYEEAKAKKEEL 374

                         170
                  ....*....|..
gi 1034594996 181 AVQQKQEKPRTP 192
Cdd:PRK03918  375 ERLKKRLTGLTP 386
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
19-181 4.51e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 38.52  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  19 KDLAMTYKQRAEnTQEELREFQEGSREYEAE---LETQLQQIETRNrdlLSENnrlrmELETIKEKFEV-QHSEGYRQ-- 92
Cdd:COG0497   158 EEYREAYRAWRA-LKKELEELRADEAERAREldlLRFQLEELEAAA---LQPG-----EEEELEEERRRlSNAEKLREal 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  93 ---ISALEDD----LAQTKAIKDQLQKYIRELEQANDDLERAKRATImSLEDFEQRLNQAIERNAFLESELDEKENLLES 165
Cdd:COG0497   229 qeaLEALSGGeggaLDLLGQALRALERLAEYDPSLAELAERLESALI-ELEEAASELRRYLDSLEFDPERLEEVEERLAL 307

                         170       180
                  ....*....|....*....|...
gi 1034594996 166 VQRLK-------DEARDLRQELA 181
Cdd:COG0497   308 LRRLArkygvtvEELLAYAEELR 330
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 5-173 4.70e-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: 38.79  E-value: 4.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   5 GKTFSSEEEEANYWKDLAMTYKQRAENTQ----EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKE 80
Cdd:COG5185   289 KQFENTKEKIAEYTKSIDIKKATESLEEQlaaaEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVG 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  81 kfevqhsegyrqISALEDDLAQTKAIKDQLQKYIRELEQANDDlerAKRATIMSLEDFEQRLNQAIERNAFLESELDEKE 160
Cdd:COG5185   369 ------------EVELSKSSEELDSFKDTIESTKESLDEIPQN---QRGYAQEILATLEDTLKAADRQIEELQRQIEQAT 433

                         170
                  ....*....|...
gi 1034594996 161 NLLESVQRLKDEA 173
Cdd:COG5185   434 SSNEEVSKLLNEL 446
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 54-252 4.92e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  54 LQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIM 133
Cdd:COG3883   124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 134 SLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSSVEAERTDTAVQATGSVP 213
Cdd:COG3883   204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAG 283

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034594996 214 STPIAHRGPSSSLNTPGSFRRGLDDSTGGTPLTPAARIS 252
Cdd:COG3883   284 GGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAV 322
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 33-174 5.22e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 38.65  E-value: 5.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  33 QEELREFQEGSREYEAELETQLQQIETrnrdLLSENNRLRMELETIKEKF-EVQHSEGYRQISALEDDLAQTKAIKDQLQ 111
Cdd:PRK00409  515 KEKLNELIASLEELERELEQKAEEAEA----LLKEAEKLKEELEEKKEKLqEEEDKLLEEAEKEAQQAIKEAKKEADEII 590

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034594996 112 KYIRELEQANDDLERAKRatimsLEDFEQRLNQAIERnafLESELDEKENLLESVQrLKDEAR 174
Cdd:PRK00409  591 KELRQLQKGGYASVKAHE-----LIEARKRLNKANEK---KEKKKKKQKEKQEELK-VGDEVK 644
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 48-234 6.75e-03

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: 37.79  E-value: 6.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  48 AELETQLQQIETRNRDLLSENNRLRMELEtikeKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERA 127
Cdd:pfam00529  54 TDYQAALDSAEAQLAKAQAQVARLQAELD----RLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996 128 K-RATI--MSLEDF-EQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQekprtpmPSSVEAERTD 203
Cdd:pfam00529 130 RvLAPIggISRESLvTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQ-------IAEAEAELKL 202

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034594996 204 TAVQATGSVPSTPIAHRGPSSSLNTPGSFRR 234
Cdd:pfam00529 203 AKLDLERTEIRAPVDGTVAFLSVTVDGGTVS 233
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
91-186 6.92e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 6.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   91 RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLN--QAIERNAFLESELDEKENLLESVQR 168
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLDASSDDLAA 689

                           90
                   ....*....|....*...
gi 1034594996  169 LKDEARDLRQELAVQQKQ 186
Cdd:COG4913    690 LEEQLEELEAELEELEEE 707
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 12-203 7.58e-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: 38.08  E-value: 7.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  12 EEEANYWKDLamtyKQRAENTQEELREFQEGSREYE---AELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSE 88
Cdd:TIGR04523 303 QKEQDWNKEL----KSELKNQEKKLEEIQNQISQNNkiiSQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  89 --GYR--------QISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDE 158
Cdd:TIGR04523 379 nqSYKqeiknlesQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN 458

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034594996 159 KENLLESVQR----LKDEARDLRQELAVQQKQEKPRTPMPSSVEAERTD 203
Cdd:TIGR04523 459 LDNTRESLETqlkvLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE 507
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 26-171 7.96e-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: 37.21  E-value: 7.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  26 KQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSE--NNR----LRMELETIKekfevqhsegyRQISALEDD 99
Cdd:COG1579    44 EARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNvrNNKeyeaLQKEIESLK-----------RRISDLEDE 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034594996 100 LAQTKAIKDQLQKYIRE----LEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDekENLLESVQRLKD 171
Cdd:COG1579   112 ILELMERIEELEEELAEleaeLAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP--PELLALYERIRK 185
PRK12704 PRK12704
phosphodiesterase; Provisional
 22-172 9.34e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.45  E-value: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  22 AMTYKQRAENTQEElrEFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETI-KEKFEVQHSEgyRQISALEDDL 100
Cdd:PRK12704   51 AEAIKKEALLEAKE--EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLeKREEELEKKE--KELEQKQQEL 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034594996 101 AQTKA-IKDQLQKYIRELEQ-ANDDLERAKRATIMSLEDfEQRLNQA-----IERNAFLESELDEKENLLESVQRLKDE 172
Cdd:PRK12704  127 EKKEEeLEELIEEQLQELERiSGLTAEEAKEILLEKVEE-EARHEAAvlikeIEEEAKEEADKKAKEILAQAIQRCAAD 204
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 26-191 9.96e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 37.64  E-value: 9.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996   26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEdDLAQTKA 105
Cdd:pfam02463  148 AMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL-ELEEEYL 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594996  106 IKDQLQKYIRELEQANDDLERAKRATIMSLedfEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:pfam02463  227 LYLDYLKLNEERIDLLQELLRDEQEEIESS---KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL 303


                   ....*.
gi 1034594996  186 QEKPRT 191
Cdd:pfam02463  304 KLERRK 309
 
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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