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Conserved domains on  [gi|530408290|ref|XP_005255453|]
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nuclear distribution protein nudE homolog 1 isoform X1 [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 3.11e-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: 173.05  E-value: 3.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  134 SLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ------EKPRTPMPSSVEAERTD 203
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKlrnllmRSPSTPSLQTLEIFDRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  204 TAVQATgsvpSTPIAHRGPSSSLNtpgSFRRGlddSTGGTPLTPAARISAlnivgDLLRKVGALESKLASCRNLVYDQSP 283
Cdd:pfam04880  81 PAVQAV----SSPVIATPPEKSFN---SLRTG---SETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNA 145
                         170       180
                  ....*....|....*....|....*.
gi 530408290  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 9.24e-09

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: 56.87  E-value: 9.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  27 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEV---QHSEGYRQISALEDDLAQT 103
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEleeELEELEEELEELEEELEEA 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 104 KAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQ 183
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429

                 ....
gi 530408290 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 3.11e-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: 173.05  E-value: 3.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  134 SLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ------EKPRTPMPSSVEAERTD 203
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKlrnllmRSPSTPSLQTLEIFDRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  204 TAVQATgsvpSTPIAHRGPSSSLNtpgSFRRGlddSTGGTPLTPAARISAlnivgDLLRKVGALESKLASCRNLVYDQSP 283
Cdd:pfam04880  81 PAVQAV----SSPVIATPPEKSFN---SLRTG---SETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNA 145
                         170       180
                  ....*....|....*....|....*.
gi 530408290  284 NRtggpasgRSSKNRDGGERRPSSTS 309
Cdd:pfam04880 146 SR-------RGNSRSLYGSRPPTKFA 164
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
27-187 9.24e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 9.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  27 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEV---QHSEGYRQISALEDDLAQT 103
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEleeELEELEEELEELEEELEEA 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 104 KAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQ 183
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429

                 ....
gi 530408290 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 1.14e-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: 56.60  E-value: 1.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    26 KQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   106 -------IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168  818 eaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897

                   ....*...
gi 530408290   179 ELAVQQKQ 186
Cdd:TIGR02168  898 ELSEELRE 905
mukB PRK04863
chromosome partition protein MukB;
41-186 1.14e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.34  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   41 EGSREYEAELETQLQQIETRnrdLLSENNRLRMElETIKEKFE------------VQHSEGYRQISALEDDLAQTKAIKD 108
Cdd:PRK04863  438 DNAEDWLEEFQAKEQEATEE---LLSLEQKLSVA-QAAHSQFEqayqlvrkiageVSRSEAWDVARELLRRLREQRHLAE 513
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  109 QLQKY---IRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:PRK04863  514 QLQQLrmrLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLE 589

                  .
gi 530408290  186 Q 186
Cdd:PRK04863  590 Q 590
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
19-188 2.33e-06

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: 48.52  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  19 KDLAMTYKQRAENTQEELREFQEGSREYeaelETQLQQIETRNRDLLSENNRL--RMELETIKEkfevqhsegyrQISAL 96
Cdd:cd22656  127 LKEAKKYQDKAAKVVDKLTDFENQTEKD----QTALETLEKALKDLLTDEGGAiaRKEIKDLQK-----------ELEKL 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  97 EDDLAqtKAIKDQLQKYIRELEQANDDLERAKR------ATIMSLEDFEQRLNQAIE-----RNAF--LESELDEKENLL 163
Cdd:cd22656  192 NEEYA--AKLKAKIDELKALIADDEAKLAAALRliadltAADTDLDNLLALIGPAIPaleklQGAWqaIATDLDSLKDLL 269
                        170       180
                 ....*....|....*....|....*
gi 530408290 164 ESVQRlkDEARDLRQELAVQQKQEK 188
Cdd:cd22656  270 EDDIS--KIPAAILAKLELEKAIEK 292
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
26-253 3.59e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 3.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLlSENNRLRMELETIKEkfevqhSEGyrqISALEDDLAQTKA 105
Cdd:COG3883   57 QAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL-YRSGGSVSYLDVLLG------SES---FSDFLDRLSALSK 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG3883  127 IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530408290 186 QEKPRTPMPSSVEAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGSFRRGLDDSTGGTPLTPAARISA 253
Cdd:COG3883  207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
48-164 3.35e-05

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 44.13  E-value: 3.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   48 AELETQLQQIETRNRDLLSENNRLRMELETIKEKFEV--QHSEGYRQISAledDLAQTKAIKDQLQKYIRELEQANDDLE 125
Cdd:pfam13851  36 AELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEElrKQLENYEKDKQ---SLKNLKARLKVLEKELKDLKWEHEVLE 112
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 530408290  126 RAKRATIMSLEDFEQRLNQAIE--------RNAFLESELDEKENLLE 164
Cdd:pfam13851 113 QRFEKVERERDELYDKFEAAIQdvqqktglKNLLLEKKLQALGETLE 159
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
142-204 1.77e-03

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 39.58  E-value: 1.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530408290 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 3.11e-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: 173.05  E-value: 3.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  134 SLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ------EKPRTPMPSSVEAERTD 203
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKlrnllmRSPSTPSLQTLEIFDRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  204 TAVQATgsvpSTPIAHRGPSSSLNtpgSFRRGlddSTGGTPLTPAARISAlnivgDLLRKVGALESKLASCRNLVYDQSP 283
Cdd:pfam04880  81 PAVQAV----SSPVIATPPEKSFN---SLRTG---SETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNA 145
                         170       180
                  ....*....|....*....|....*.
gi 530408290  284 NRtggpasgRSSKNRDGGERRPSSTS 309
Cdd:pfam04880 146 SR-------RGNSRSLYGSRPPTKFA 164
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
27-187 9.24e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 9.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  27 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEV---QHSEGYRQISALEDDLAQT 103
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEleeELEELEEELEELEEELEEA 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 104 KAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQ 183
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429

                 ....
gi 530408290 184 QKQE 187
Cdd:COG1196  430 LAEL 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
26-188 9.49e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 9.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  26 KQRAENTQEELREFQEGSREYEAELEtQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQ----RLKDEARDLRQELA 181
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLerleRLEEELEELEEALA 431

                 ....*..
gi 530408290 182 VQQKQEK 188
Cdd:COG1196  432 ELEEEEE 438
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
26-186 1.14e-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: 56.60  E-value: 1.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    26 KQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   106 -------IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168  818 eaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897

                   ....*...
gi 530408290   179 ELAVQQKQ 186
Cdd:TIGR02168  898 ELSEELRE 905
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
11-188 1.44e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  11 EEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGY 90
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  91 RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLK 170
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
                        170
                 ....*....|....*...
gi 530408290 171 DEARDLRQELAVQQKQEK 188
Cdd:COG1196  460 ALLELLAELLEEAALLEA 477
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
26-187 1.93e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477

                 ..
gi 530408290 186 QE 187
Cdd:COG1196  478 AL 479
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
24-188 2.85e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 2.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  24 TYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRM------ELETIKEKFEVQHSEGYRQISALE 97
Cdd:COG1196  243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaelaRLEQDIARLEERRRELEERLEELE 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  98 DDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLR 177
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE---LAEAEEELEELAEELLEALRAAAELA 399
                        170
                 ....*....|.
gi 530408290 178 QELAVQQKQEK 188
Cdd:COG1196  400 AQLEELEEAEE 410
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
26-187 3.98e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 3.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHsegyRQISALEDDLAQTKA 105
Cdd:COG1196  329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL----EALRAAAELAAQLEE 404
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196  405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484

                 ..
gi 530408290 186 QE 187
Cdd:COG1196  485 EL 486
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
27-201 7.61e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 7.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   27 QRAENTQEELREFQEGSREYEAE-----LETQLQQIETRNRDLLSENNRLRMELETIKEK---FEVQHSE-GYRQISALE 97
Cdd:COG4913   265 AAARERLAELEYLRAALRLWFAQrrlelLEAELEELRAELARLEAELERLEARLDALREEldeLEAQIRGnGGDRLEQLE 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   98 DDLAQTKAIKDQLQkyiRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEN----LLESVQRLKDEA 173
Cdd:COG4913   345 REIERLERELEERE---RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRREL 421
                         170       180
                  ....*....|....*....|....*...
gi 530408290  174 RDLRQELAVQQKQekpRTPMPSSVEAER 201
Cdd:COG4913   422 RELEAEIASLERR---KSNIPARLLALR 446
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
34-186 1.22e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 1.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    34 EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYR---QISALEDDLAQTKAIKDQL 110
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARleaEVEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530408290   111 QKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEARDLRQELAVQQKQ 186
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR---AELTLLNEEAANLRERLESLERR 832
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-200 1.53e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   48 AELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVqhSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERA 127
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREA--LQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAAL 690
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530408290  128 KR---ATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSSVEAE 200
Cdd:COG4913   691 EEqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
27-188 1.60e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  27 QRAENTQEELREFQEGSREYeAELETQLQQIETRNRDLLSENNRLRMELETIKEkfEVQHSEGYRQISALEDDLAQTKAI 106
Cdd:COG4717   71 KELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEKLEK--LLQLLPLYQELEALEAELAELPER 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 107 KDQLQKYIRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAF-----LESELDEKENLLESVQRLKDEARDLRQELA 181
Cdd:COG4717  148 LEELEERLEELRELEEELEELEAE----LAELQEELEELLEQLSLateeeLQDLAEELEELQQRLAELEEELEEAQEELE 223

                 ....*..
gi 530408290 182 VQQKQEK 188
Cdd:COG4717  224 ELEEELE 230
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
26-188 2.01e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEvqhsegyrqisALEDDLAQTKA 105
Cdd:COG1196  297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE-----------EAEAELAEAEE 365
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196  366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA---EEALLERLERLEEELEELEEALAELEEEEEEEEE 442

                 ...
gi 530408290 186 QEK 188
Cdd:COG1196  443 ALE 445
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
26-216 3.38e-07

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: 51.30  E-value: 3.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  26 KQRAENTQEELREFQEGSREYEA---ELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQ---------- 92
Cdd:COG4942   47 KKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalll 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  93 ----ISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLesvQR 168
Cdd:COG4942  127 spedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL---AR 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 530408290 169 LKDEARDLRQELAVQQKQEKPRTPMPSSVEAERTDTAVQATGSVPSTP 216
Cdd:COG4942  204 LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
30-188 4.18e-07

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: 51.56  E-value: 4.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   30 ENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRL---RMELETIK-EKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLnqlKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQN 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  106 IKDQLQKYIRELEQANDDLERakraTIMSLEDFEQRLNQAI-ERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQ 184
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKK----ELTNSESENSEKQRELeEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404

                  ....
gi 530408290  185 KQEK 188
Cdd:TIGR04523 405 KLNQ 408
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
48-188 4.92e-07

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: 49.92  E-value: 4.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  48 AELETQLQQIETRNRDLLSENNRLRMELETIK---EKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYI------RELE 118
Cdd:COG1579   13 QELDSELDRLEHRLKELPAELAELEDELAALEarlEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnKEYE 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530408290 119 QANDDLERAKRAtIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQ-RLKDEARDLRQELAVQQKQEK 188
Cdd:COG1579   93 ALQKEIESLKRR-ISDLEDEILELMERIEE---LEEELAELEAELAELEaELEEKKAELDEELAELEAELE 159
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
24-186 6.00e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.17  E-value: 6.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  24 TYKQRAENTQEELREFQEGSREYE------------AELETQLQQIETRNRDLLSENNRLRMELETIKEkfEVQHSEGYR 91
Cdd:COG3206  186 ELRKELEEAEAALEEFRQKNGLVDlseeaklllqqlSELESQLAEARAELAEAEARLAALRAQLGSGPD--ALPELLQSP 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  92 QISALEDDLAQTKA-IKDQLQKY------IRELEQANDDLERAKRATI-MSLEDFEQRLNQAIERNAFLESELDEKENLL 163
Cdd:COG3206  264 VIQQLRAQLAELEAeLAELSARYtpnhpdVIALRAQIAALRAQLQQEAqRILASLEAELEALQAREASLQAQLAQLEARL 343
                        170       180
                 ....*....|....*....|...
gi 530408290 164 ESVQRLKDEARDLRQELAVQQKQ 186
Cdd:COG3206  344 AELPELEAELRRLEREVEVAREL 366
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
26-181 6.02e-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: 51.21  E-value: 6.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    26 KQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIE-ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL------------ESVQRLKDEA 173
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaealenkieDDEEEARRRL 974

                   ....*...
gi 530408290   174 RDLRQELA 181
Cdd:TIGR02168  975 KRLENKIK 982
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
19-181 8.12e-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: 8.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    19 KDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSegyrQISALED 98
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN----EIERLEA 407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    99 DLAQtkaIKDQLQKYIRELEQANDDLERAKRATI-MSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLR 177
Cdd:TIGR02168  408 RLER---LEDRRERLQQEIEELLKKLEEAELKELqAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484

                   ....
gi 530408290   178 QELA 181
Cdd:TIGR02168  485 AQLQ 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
26-187 9.63e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 9.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRnrdlLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196  346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE----LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196  422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501

                 ..
gi 530408290 186 QE 187
Cdd:COG1196  502 DY 503
mukB PRK04863
chromosome partition protein MukB;
41-186 1.14e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.34  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   41 EGSREYEAELETQLQQIETRnrdLLSENNRLRMElETIKEKFE------------VQHSEGYRQISALEDDLAQTKAIKD 108
Cdd:PRK04863  438 DNAEDWLEEFQAKEQEATEE---LLSLEQKLSVA-QAAHSQFEqayqlvrkiageVSRSEAWDVARELLRRLREQRHLAE 513
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  109 QLQKY---IRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:PRK04863  514 QLQQLrmrLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLE 589

                  .
gi 530408290  186 Q 186
Cdd:PRK04863  590 Q 590
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
27-180 1.33e-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: 50.06  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    27 QRAENTQEELREFQEGS-----REYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKfEVQHSEGYRQISALEDDLA 101
Cdd:TIGR02168  213 ERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELEEEIEELQKELY 291
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530408290   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 1.35e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 1.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    11 EEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEA-----------------ELETQLQQIETRNRDLLSENNRLRM 73
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAalrdlesrlgdlkkerdELEAQLRELERKIEELEAQIEKKRK 917
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    74 ELETIKEKFEVQHSEgyrqISALEDDLAQTKAIK------DQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIE 147
Cdd:TIGR02169  918 RLSELKAKLEALEEE----LSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993
                          170       180
                   ....*....|....*....|....*.
gi 530408290   148 RNAFLESELDEKENLLESVQRLKDEA 173
Cdd:TIGR02169  994 KRAKLEEERKAILERIEEYEKKKREV 1019
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1-188 1.80e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 1.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290     1 MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLlsenNRLRMELETIK- 79
Cdd:TIGR02169  711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEa 786
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    80 --------------EKFEVQHSEGYRQISALEDDLAQTKAIKDQLQK-------YIRELE-------QANDDLERAKRAT 131
Cdd:TIGR02169  787 rlshsripeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKeiqelqeQRIDLKeqiksieKEIENLNGKKEEL 866
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530408290   132 IMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 188
Cdd:TIGR02169  867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1-191 2.21e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290     1 MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEA---ELETQLQQIETRNRDLLSENNRLRMELET 77
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESkrsELRRELEELREKLAQLELRLEGLEVRIDN 940
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    78 IKEKFevqhSEGYRqiSALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQrLNqaiERNAFLESELD 157
Cdd:TIGR02168  941 LQERL----SEEYS--LTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEE-LK---ERYDFLTAQKE 1010
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 530408290   158 E----KENLLESVQRLKDEARDLRQELAVQQKQEKPRT 191
Cdd:TIGR02168 1011 DlteaKETLEEAIEEIDREARERFKDTFDQVNENFQRV 1048
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
19-188 2.33e-06

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: 48.52  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  19 KDLAMTYKQRAENTQEELREFQEGSREYeaelETQLQQIETRNRDLLSENNRL--RMELETIKEkfevqhsegyrQISAL 96
Cdd:cd22656  127 LKEAKKYQDKAAKVVDKLTDFENQTEKD----QTALETLEKALKDLLTDEGGAiaRKEIKDLQK-----------ELEKL 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  97 EDDLAqtKAIKDQLQKYIRELEQANDDLERAKR------ATIMSLEDFEQRLNQAIE-----RNAF--LESELDEKENLL 163
Cdd:cd22656  192 NEEYA--AKLKAKIDELKALIADDEAKLAAALRliadltAADTDLDNLLALIGPAIPaleklQGAWqaIATDLDSLKDLL 269
                        170       180
                 ....*....|....*....|....*
gi 530408290 164 ESVQRlkDEARDLRQELAVQQKQEK 188
Cdd:cd22656  270 EDDIS--KIPAAILAKLELEKAIEK 292
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
24-187 2.83e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 2.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    24 TYKQRAENTQEELREFQEGSREYEAELET----------QLQQIETRNRDLLSENNRLRMELETIKEKF----------E 83
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQELEEKLEElrlevseleeEIEELQKELYALANEISRLEQQKQILRERLanlerqleelE 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    84 VQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQAND-------DLERAKRATIMSLEDFEQRLNQAIERNAFLESEL 156
Cdd:TIGR02168  323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 530408290   157 ----DEKENLLESVQRLKDEARDLRQELAVQQKQE 187
Cdd:TIGR02168  403 erleARLERLEDRRERLQQEIEELLKKLEEAELKE 437
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
47-191 2.96e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 2.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  47 EAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEgYRQisaLEDDLAQTKAIKDQLQKYIRELEQANDDLER 126
Cdd:COG4717   48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEE-YAE---LQEELEELEEELEELEAELEELREELEKLEK 123
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530408290 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 3.33e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.91  E-value: 3.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    27 QRAENTQEELREFQEGSREYEA--------ELETQLQQIETRnrdllsennrlRMELETIKEKFEVQHSEGYRQISALED 98
Cdd:TIGR02169  204 RREREKAERYQALLKEKREYEGyellkekeALERQKEAIERQ-----------LASLEEELEKLTEEISELEKRLEEIEQ 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    99 DLAQ-TKAIKD-------QLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELD-----------EK 159
Cdd:TIGR02169  273 LLEElNKKIKDlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEelereieeerkRR 352
                          170       180
                   ....*....|....*....|..
gi 530408290   160 ENLLESVQRLKDEARDLRQELA 181
Cdd:TIGR02169  353 DKLTEEYAELKEELEDLRAELE 374
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
26-253 3.59e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 3.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLlSENNRLRMELETIKEkfevqhSEGyrqISALEDDLAQTKA 105
Cdd:COG3883   57 QAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL-YRSGGSVSYLDVLLG------SES---FSDFLDRLSALSK 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG3883  127 IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530408290 186 QEKPRTPMPSSVEAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGSFRRGLDDSTGGTPLTPAARISA 253
Cdd:COG3883  207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
25-188 4.38e-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: 4.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    25 YKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSEN---NRLRMELETIKEKFEVQHS---EGYRQISALED 98
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRealDELRAELTLLNEEAANLRErleSLERRIAATER 838
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    99 DLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
                          170
                   ....*....|
gi 530408290   179 ELAVQQKQEK 188
Cdd:TIGR02168  919 ELREKLAQLE 928
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-196 4.85e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 4.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   48 AELETQLQQIETRNRDLLSENNRLRmELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQkyiRELEQANDDLERA 127
Cdd:COG4913   664 ASAEREIAELEAELERLDASSDDLA-ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE---EELDELQDRLEAA 739
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  128 -KRATIMSLEDFEQRLNQAIERNAflesELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSS 196
Cdd:COG4913   740 eDLARLELRALLEERFAAALGDAV----ERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETA 805
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
24-196 6.05e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 6.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  24 TYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFevqhSEGYRQISALEDDLAQT 103
Cdd:COG4942   73 ALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDF----LDAVRRLQYLKYLAPAR 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 104 KAIKDQLQKYIRELEQANDDLERAK---RATIMSLEDFEQRLNQAIERNAFLESELDEKENLLES-VQRLKDEARDLRQE 179
Cdd:COG4942  149 REQAEELRADLAELAALRAELEAERaelEALLAELEEERAALEALKAERQKLLARLEKELAELAAeLAELQQEAEELEAL 228
                        170
                 ....*....|....*..
gi 530408290 180 LAVQQKQEKPRTPMPSS 196
Cdd:COG4942  229 IARLEAEAAAAAERTPA 245
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
37-187 2.21e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 2.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  37 REFQEGSREYEAEL--------ETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYR---QISALEDDLAQTKA 105
Cdd:COG1196  216 RELKEELKELEAELlllklrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEElelELEEAQAEEYELLA 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 106 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                 ..
gi 530408290 186 QE 187
Cdd:COG1196  376 EA 377
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
95-186 2.24e-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: 45.91  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  95 ALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEAR 174
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEIA 93
                         90
                 ....*....|..
gi 530408290 175 DLRQELAVQQKQ 186
Cdd:COG4942   94 ELRAELEAQKEE 105
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
48-164 3.35e-05

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 44.13  E-value: 3.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   48 AELETQLQQIETRNRDLLSENNRLRMELETIKEKFEV--QHSEGYRQISAledDLAQTKAIKDQLQKYIRELEQANDDLE 125
Cdd:pfam13851  36 AELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEElrKQLENYEKDKQ---SLKNLKARLKVLEKELKDLKWEHEVLE 112
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 530408290  126 RAKRATIMSLEDFEQRLNQAIE--------RNAFLESELDEKENLLE 164
Cdd:pfam13851 113 QRFEKVERERDELYDKFEAAIQdvqqktglKNLLLEKKLQALGETLE 159
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
12-176 3.49e-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: 3.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    12 EEEANYWKDLamtyKQRAENTQEELREFQEGSREYEAELET---QLQQIETRNRDLLSENNRLRMELETIKEKFEVQhse 88
Cdd:TIGR02168  361 EELEAELEEL----ESRLEELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQEIEELLKKLEEA--- 433
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    89 gyrQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQR 168
Cdd:TIGR02168  434 ---ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510

                   ....*...
gi 530408290   169 LKDEARDL 176
Cdd:TIGR02168  511 LLKNQSGL 518
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
20-190 4.34e-05

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 45.60  E-value: 4.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    20 DLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSE------GYRQ- 92
Cdd:pfam12128  643 FARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREartekqAYWQv 722
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    93 -ISALEDDLAQTKAIKDQLQ------------KYIREL------EQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLE 153
Cdd:pfam12128  723 vEGALDAQLALLKAAIAARRsgakaelkaletWYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQ 802
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 530408290   154 SE-LDEKENLLESVQRLKDEARDLRQELAVQQKQEKPR 190
Cdd:pfam12128  803 ETwLQRRPRLATQLSNIERAISELQQQLARLIADTKLR 840
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-187 5.54e-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: 45.05  E-value: 5.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290     4 SGKTFSSEEEEANYWKDLAMTyKQRAENTQEELREFQEGSREYEAELE---TQLQQIETRNRDLLSENNRLRMELETIKE 80
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEEL-EEKIAELEKALAELRKELEELEEELEqlrKELEELSRQISALRKDLARLEAEVEQLEE 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    81 K----------FEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNA 150
Cdd:TIGR02168  748 RiaqlskelteLEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 530408290   151 FLESELDEKENLLESVQRLKDEARDLRQELAVQQKQE 187
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
91-163 9.36e-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: 9.36e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530408290  91 RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL 163
Cdd:COG4942   34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
24-190 1.25e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  24 TYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRD-----LLSENNRLRMELETIKEKFEVQHSegyrQISALED 98
Cdd:COG3206  223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpviqqLRAQLAELEAELAELSARYTPNHP----DVIALRA 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  99 DLAQTKA-IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIErnafLESELDEKENLLESVQRLKDEARDLR 177
Cdd:COG3206  299 QIAALRAqLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELYESLLQRL 374
                        170
                 ....*....|...
gi 530408290 178 QELAVQQKQEKPR 190
Cdd:COG3206  375 EEARLAEALTVGN 387
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
26-174 1.30e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  26 KQRAENTQEELREFQEgsrEYEAeLETQLQQIETRNRDLLSENNRLRMELETIK---EKFEVQHSEG--YRQISALEDDL 100
Cdd:COG1579   23 EHRLKELPAELAELED---ELAA-LEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLGNVrnNKEYEALQKEI 98
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530408290 101 AQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEAR 174
Cdd:COG1579   99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELA 169
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
19-188 1.66e-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: 43.57  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    19 KDLAMTYKQRAENTQEEL-REFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALE 97
Cdd:pfam15921  244 EDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLE 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    98 DDLAQtkaIKDQLQKYIRELEQANDDLEraKRATIMSLEDFEQRlnqaIERNAFLEseldEKENLLESVQRLKDEARDLR 177
Cdd:pfam15921  324 STVSQ---LRSELREAKRMYEDKIEELE--KQLVLANSELTEAR----TERDQFSQ----ESGNLDDQLQKLLADLHKRE 390
                          170
                   ....*....|.
gi 530408290   178 QELAVQQKQEK 188
Cdd:pfam15921  391 KELSLEKEQNK 401
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
27-176 1.76e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  27 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAI 106
Cdd:COG1196  682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530408290 107 KDQLQKYIRELEQANDDLE----RAkratimsLEDFEqrlnQAIERNAFLESELD----EKENLLESVQRLKDEARDL 176
Cdd:COG1196  762 LEELERELERLEREIEALGpvnlLA-------IEEYE----ELEERYDFLSEQREdleeARETLEEAIEEIDRETRER 828
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
12-203 2.34e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   12 EEEANYWKDLamtyKQRAENTQEELREFQEGSREYE---AELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSE 88
Cdd:TIGR04523 303 QKEQDWNKEL----KSELKNQEKKLEEIQNQISQNNkiiSQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   89 --GYR--------QISALEDDLAQTKAIKDQLQKYIRELEQANDDLERakraTIMSLEDFEQRLNQAIERnafLESELDE 158
Cdd:TIGR04523 379 nqSYKqeiknlesQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK----EIERLKETIIKNNSEIKD---LTNQDSV 451
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530408290  159 KENLLESVQRLKD-----------EARDLRQELAVQQKQEKPRTPMPSSVEAERTD 203
Cdd:TIGR04523 452 KELIIKNLDNTREsletqlkvlsrSINKIKQNLEQKQKELKSKEKELKKLNEEKKE 507
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
40-190 2.39e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.02  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   40 QEGSREYEAELETQLQQIETRNRDL-----LSENNRLRME-----LETIKEkfEVQHSEGY-------RQISALEDDLAQ 102
Cdd:COG3096   436 PENAEDYLAAFRAKEQQATEEVLELeqklsVADAARRQFEkayelVCKIAG--EVERSQAWqtarellRRYRSQQALAQR 513
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  103 TKAIKDQLqkyiRELEQANDDLERAKRatimSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAV 182
Cdd:COG3096   514 LQQLRAQL----AELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585

                  ....*...
gi 530408290  183 QQKQEKPR 190
Cdd:COG3096   586 QLEQLRAR 593
PRK14160 PRK14160
heat shock protein GrpE; Provisional
1-188 2.55e-04

heat shock protein GrpE; Provisional


Pssm-ID: 237629 [Multi-domain]  Cd Length: 211  Bit Score: 41.66  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   1 MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREF--QEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETI 78
Cdd:PRK14160   1 MEKECKDAKHENMEEDCCKENENKEEDKGKEEDLEFEEIekEEIIEDSEESNEVKIEELKDENNKLKEENKKLENELEAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  79 KEKFE--VQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELeqanDDLERAKrATIMSLEDFEQRLNQAIE--RNAF--- 151
Cdd:PRK14160  81 KDRLLrtVAEYDNYRKRTAKEKEGIYSDACEDVLKELLPVL----DNLERAA-AVEGSVEDLKKGIEMTVKqfKTSLekl 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 530408290 152 ----LESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 188
Cdd:PRK14160 156 gveeISTEGEFDPNLHNAVMHVEDENYGENEIVEVFQKGYK 196
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
5-173 2.86e-04

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 42.64  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   5 GKTFSSEEEEANYWKDLAMTYKQRAENTQ----EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIke 80
Cdd:COG5185  289 KQFENTKEKIAEYTKSIDIKKATESLEEQlaaaEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENI-- 366
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  81 kfevqhsEGYRQISALEDDLaqtKAIKDQLQKYIRELEQANDDlerAKRATIMSLEDFEQRLNQAIERNAFLESELDEKE 160
Cdd:COG5185  367 -------VGEVELSKSSEEL---DSFKDTIESTKESLDEIPQN---QRGYAQEILATLEDTLKAADRQIEELQRQIEQAT 433
                        170
                 ....*....|...
gi 530408290 161 NLLESVQRLKDEA 173
Cdd:COG5185  434 SSNEEVSKLLNEL 446
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
49-189 2.96e-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: 42.74  E-value: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    49 ELETQLQQIETR--NRDLLSENNRLRmELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLER 126
Cdd:TIGR02168  217 ELKAELRELELAllVLRLEELREELE-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530408290   127 AkratimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKP 189
Cdd:TIGR02168  296 E-------ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
26-171 2.98e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  26 KQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSE--NNR----LRMELETIKekfevqhsegyRQISALEDD 99
Cdd:COG1579   44 EARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNvrNNKeyeaLQKEIESLK-----------RRISDLEDE 111
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530408290 100 LAQTKAIKDQLQKYIRE----LEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDekENLLESVQRLKD 171
Cdd:COG1579  112 ILELMERIEELEEELAEleaeLAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP--PELLALYERIRK 185
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
12-180 3.00e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  12 EEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELEtQLQQIetrnRDLLSENNRLRMELETIKEKFEVQH----- 86
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERI----RTLLAAIADAEDEIERLREKREALAelnde 624
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  87 -----SEGYRQISALEDD-----LAQTKAIKDQLQKYIRELEQANDDLERAK---RATIMSLEDFEQRLNQAIERNAFLE 153
Cdd:PRK02224 625 rrerlAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERddlQAEIGAVENELEELEELRERREALE 704
                        170       180
                 ....*....|....*....|....*..
gi 530408290 154 SELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:PRK02224 705 NRVEALEALYDEAEELESMYGDLRAEL 731
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
33-184 3.23e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 3.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    33 QEELREFQEGSREYEAELETQLQQIETRNRDLlsenNRLRMELETIKEKFEvqhsEGYRQISALEDDLAQTKAIKDQLQK 112
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSDASRKIGEIEKEI----EQLEQEEEKLKERLE----ELEEDLSSLEQEIENVKSELKELEA 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   113 YIRELEQANDDLERAkratimsLEDFEQRLNQAI------------ERNAFLESELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:TIGR02169  766 RIEELEEDLHKLEEA-------LNDLEARLSHSRipeiqaelskleEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838

                   ....
gi 530408290   181 AVQQ 184
Cdd:TIGR02169  839 QEQR 842
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
21-190 3.45e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.42  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   21 LAMTYKQRAENTQEELREFQ-EGSREYEAELE-TQLQQIETRNRDLLSENNRLRMELETIKeKFEVQHSEGYRQISALED 98
Cdd:pfam17380 342 MAMERERELERIRQEERKRElERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAAR-KVKILEEERQRKIQQQKV 420
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   99 DLAQTKAIKDQL-QKYIRELEQanddlERAKRATIMSLEDFEQRlnQAIERNAFLESELDEKENLLESVQRLKDEARDLR 177
Cdd:pfam17380 421 EMEQIRAEQEEArQREVRRLEE-----ERAREMERVRLEEQERQ--QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR 493
                         170
                  ....*....|...
gi 530408290  178 QELAVQQKQEKPR 190
Cdd:pfam17380 494 RKILEKELEERKQ 506
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
28-187 4.59e-04

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: 41.80  E-value: 4.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   28 RAENTQEELrefqEGSREYEAELetqLQQIETRNRDLLSEnnrlRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIK 107
Cdd:pfam07888  28 RAELLQNRL----EECLQERAEL---LQAQEAANRQREKE----KERYKRDREQWERQRRELESRVAELKEELRQSREKH 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  108 DQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLEsvqRLKDEARdlrqELAVQQKQE 187
Cdd:pfam07888  97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE---RMKERAK----KAGAQRKEE 169
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
12-186 4.77e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 4.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  12 EEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELET----------QLQQIETRNRDLLSENNRLR-------ME 74
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEElrerfgdapvDLGNAEDFLEELREERDELRereaeleAT 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  75 LETIKEKFEV--------------QHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKratimSLEDFEQ 140
Cdd:PRK02224 435 LRTARERVEEaealleagkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-----DLVEAED 509
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 530408290 141 RLNQAIERNAFLESELDEKENLLES----VQRLKDEARDLRQELAVQQKQ 186
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEkrerAEELRERAAELEAEAEEKREA 559
PilN COG3166
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
138-193 5.23e-04

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


Pssm-ID: 442399 [Multi-domain]  Cd Length: 185  Bit Score: 40.34  E-value: 5.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530408290 138 FEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPM 193
Cdd:COG3166   43 LQGQIAQQQARNAALQQEIAKLDKQIAEIKELKKQKAELLARLQVIEQLQQSRPPW 98
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
34-192 6.48e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 6.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  34 EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEkFEVQHSEGYRQISALEDDLAQTKAIKDQLQKY 113
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE-LEERIEELKKEIEELEEKVKELKELKEKAEEY 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 114 IReLEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLES-------------ELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:PRK03918 296 IK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeerleelkkklkELEKRLEELEERHELYEEAKAKKEEL 374
                        170
                 ....*....|..
gi 530408290 181 AVQQKQEKPRTP 192
Cdd:PRK03918 375 ERLKKRLTGLTP 386
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
19-180 7.64e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 7.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    19 KDLAMTYKQRAEnTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALED 98
Cdd:TIGR02169  237 RQKEAIERQLAS-LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    99 DLAQTKAIKDQLQKYIRELEQANDDLERakratimSLEDFEQRLNQAIERNAFLESELDEKENLLESV----QRLKDEAR 174
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEELER-------EIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefAETRDELK 388

                   ....*.
gi 530408290   175 DLRQEL 180
Cdd:TIGR02169  389 DYREKL 394
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
26-191 8.70e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.50  E-value: 8.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290    26 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEdDLAQTKA 105
Cdd:pfam02463  148 AMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL-ELEEEYL 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   106 IKDQLQKYIRELEQANDDLERAKRATIMSLedfEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:pfam02463  227 LYLDYLKLNEERIDLLQELLRDEQEEIESS---KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL 303

                   ....*.
gi 530408290   186 QEKPRT 191
Cdd:pfam02463  304 KLERRK 309
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
19-181 1.33e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.44  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  19 KDLAMTYKQRAEnTQEELREFQEGSREYEAE---LETQLQQIETRNrdlLSENnrlrmELETIKEKFEV-QHSEGYRQ-- 92
Cdd:COG0497  158 EEYREAYRAWRA-LKKELEELRADEAERAREldlLRFQLEELEAAA---LQPG-----EEEELEEERRRlSNAEKLREal 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  93 ---ISALEDD----LAQTKAIKDQLQKYIRELEQANDDLERAKRATImSLEDFEQRLNQAIERNAFLESELDEKENLLES 165
Cdd:COG0497  229 qeaLEALSGGeggaLDLLGQALRALERLAEYDPSLAELAERLESALI-ELEEAASELRRYLDSLEFDPERLEEVEERLAL 307
                        170       180
                 ....*....|....*....|...
gi 530408290 166 VQRLK-------DEARDLRQELA 181
Cdd:COG0497  308 LRRLArkygvtvEELLAYAEELR 330
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
16-198 1.38e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  16 NYWKDLA---MTYKQRAENTQEELR---EFQEGSREYEAELETQLQQI---ETRNRDLLSENNRLRMELETIKEKFEvQH 86
Cdd:PRK03918 162 NAYKNLGeviKEIKRRIERLEKFIKrteNIEELIKEKEKELEEVLREIneiSSELPELREELEKLEKEVKELEELKE-EI 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  87 SEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLE-RAKRatimsLEDFEQRLNQAIERNAFLESELDEKenlles 165
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEeKVKE-----LKELKEKAEEYIKLSEFYEEYLDEL------ 309
                        170       180       190
                 ....*....|....*....|....*....|...
gi 530408290 166 vQRLKDEARDLRQELAVQQKQEKPRTPMPSSVE 198
Cdd:PRK03918 310 -REIEKRLSRLEEEINGIEERIKELEEKEERLE 341
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
54-252 1.62e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  54 LQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIM 133
Cdd:COG3883  124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 134 SLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSSVEAERTDTAVQATGSVP 213
Cdd:COG3883  204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAG 283
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 530408290 214 STPIAHRGPSSSLNTPGSFRRGLDDSTGGTPLTPAARIS 252
Cdd:COG3883  284 GGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAV 322
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
25-188 1.68e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   25 YKQRAENTQEELREFQEGSREYEAELETQLQQIETRN---RDLLSENNRLRMELETIKEKFEVQHsegyRQISALEDdla 101
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNseiKDLTNQDSVKELIIKNLDNTRESLE----TQLKVLSR--- 475
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  102 QTKAIKDQLQKYIRELEQANDDLERAKRATIMS---LEDFEQRLNQAIERNAFLESELDEKENLLESvqrLKDEARDLRQ 178
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELeekVKDLTKKISSLKEKIEKLESEKKEKESKISD---LEDELNKDDF 552
                         170
                  ....*....|....*..
gi 530408290  179 EL-------AVQQKQEK 188
Cdd:TIGR04523 553 ELkkenlekEIDEKNKE 569
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
26-174 1.72e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  26 KQRAENTQE-----ELREFQEGSREYEAELET------QLQQIETRNRDLLSENNRLRMELEtikEKFEVQHSEGYRQis 94
Cdd:PRK02224 579 SKLAELKERiesleRIRTLLAAIADAEDEIERlrekreALAELNDERRERLAEKRERKRELE---AEFDEARIEEARE-- 653
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  95 aledDLAQTKAIKDQLQKYIRELEQANDDLER---AKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKD 171
Cdd:PRK02224 654 ----DKERAEEYLEQVEEKLDELREERDDLQAeigAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRA 729

                 ...
gi 530408290 172 EAR 174
Cdd:PRK02224 730 ELR 732
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
142-204 1.77e-03

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 39.58  E-value: 1.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530408290 142 LNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVqqKQEKPRTPMPSSVEAERTDT 204
Cdd:PRK13922  71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNL--KESLDYQFITARVISRSPDP 131
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
44-79 1.79e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 39.82  E-value: 1.79e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 530408290  44 REYEAELETQLQQIETRNRDLLSENNRLRMELETIK 79
Cdd:PRK03992   7 EERNSELEEQIRQLELKLRDLEAENEKLERELERLK 42
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
48-234 1.81e-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: 39.71  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   48 AELETQLQQIETRnrdllsennrlRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERA 127
Cdd:pfam00529  61 DSAEAQLAKAQAQ-----------VARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARR 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  128 K-RATI--MSLEDF-EQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQekprtpmPSSVEAERTD 203
Cdd:pfam00529 130 RvLAPIggISRESLvTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQ-------IAEAEAELKL 202
                         170       180       190
                  ....*....|....*....|....*....|.
gi 530408290  204 TAVQATGSVPSTPIAHRGPSSSLNTPGSFRR 234
Cdd:pfam00529 203 AKLDLERTEIRAPVDGTVAFLSVTVDGGTVS 233
mukB PRK04863
chromosome partition protein MukB;
22-188 2.23e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   22 AMTYKQRAENTQEELREFQEgsREYEAEL---ETQLQQIETRNRDLLSEN--NRLRMELETIKEKFEVQHSEG--YRQ-I 93
Cdd:PRK04863  343 ALRQQEKIERYQADLEELEE--RLEEQNEvveEADEQQEENEARAEAAEEevDELKSQLADYQQALDVQQTRAiqYQQaV 420
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   94 SALE--------DDLAQTKAIK--DQLQKYIRELEQANDDLERAKRATIMSLEDFEQ------RLNQAIERNAF------ 151
Cdd:PRK04863  421 QALErakqlcglPDLTADNAEDwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayqlvrKIAGEVSRSEAwdvare 500
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 530408290  152 LESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 188
Cdd:PRK04863  501 LLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAER 537
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
34-187 2.27e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  34 EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKfeVQHSEgyrQISALEDDLAQTKAIKDQLQKY 113
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK--VKELK---ELKEKAEEYIKLSEFYEEYLDE 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 114 IRELEQANDDLE---RAKRATIMSLEDFEQRLNQAIERNAFLE---SELDEKENLLESVQRLKDEARDLRQELAVQQKQE 187
Cdd:PRK03918 309 LREIEKRLSRLEeeiNGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTGLTPEK 388
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
91-186 2.56e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   91 RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLN--QAIERNAFLESELDEKENLLESVQR 168
Cdd:COG4913   610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLDASSDDLAA 689
                          90
                  ....*....|....*...
gi 530408290  169 LKDEARDLRQELAVQQKQ 186
Cdd:COG4913   690 LEEQLEELEAELEELEEE 707
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
33-174 3.31e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.42  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  33 QEELREFQEGSREYEAELETQLQQIETrnrdLLSENNRLRMELETIKEKF-EVQHSEGYRQISALEDDLAQTKAIKDQLQ 111
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEA----LLKEAEKLKEELEEKKEKLqEEEDKLLEEAEKEAQQAIKEAKKEADEII 590
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530408290 112 KYIRELEQANDDLERAKRatimsLEDFEQRLNQAIERnafLESELDEKENLLESVQrLKDEAR 174
Cdd:PRK00409 591 KELRQLQKGGYASVKAHE-----LIEARKRLNKANEK---KEKKKKKQKEKQEELK-VGDEVK 644
PRK12704 PRK12704
phosphodiesterase; Provisional
22-172 3.50e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  22 AMTYKQRAENTQEElrEFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETI-KEKFEVQHSEgyRQISALEDDL 100
Cdd:PRK12704  51 AEAIKKEALLEAKE--EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLeKREEELEKKE--KELEQKQQEL 126
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530408290 101 AQTKA-IKDQLQKYIRELEQ-ANDDLERAKRATIMSLEDfEQRLNQA-----IERNAFLESELDEKENLLESVQRLKDE 172
Cdd:PRK12704 127 EKKEEeLEELIEEQLQELERiSGLTAEEAKEILLEKVEE-EARHEAAvlikeIEEEAKEEADKKAKEILAQAIQRCAAD 204
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-190 4.06e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  21 LAMTYKQRAENTQEELREFQEGSREYEAELE---TQLQQIETRNRDLLSENNRLRMELETIKEKFEvqhsEGYRQISALE 97
Cdd:COG4372   25 LIAALSEQLRKALFELDKLQEELEQLREELEqarEELEQLEEELEQARSELEQLEEELEELNEQLQ----AAQAELAQAQ 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  98 DDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQR--LKDEARD 175
Cdd:COG4372  101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelQALSEAE 180
                        170
                 ....*....|....*
gi 530408290 176 LRQELAVQQKQEKPR 190
Cdd:COG4372  181 AEQALDELLKEANRN 195
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
97-176 4.64e-03

cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.


Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 36.13  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   97 EDDLAQTKAIKDQLQKYIRELEQANDDLERA---------KRATIMSLEDFEQRlnqAIERNAF-LESELDEKENLLESV 166
Cdd:pfam15898   7 EEELQENERLKRKLQDAQQELAELKSQLERLtqqrqesfsDRSSLLETEKREKR---ALERKISeMEEELKVLEDLRAEN 83
                          90
                  ....*....|
gi 530408290  167 QRLKDEARDL 176
Cdd:pfam15898  84 QRLKDENGAL 93
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
10-179 4.80e-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: 4.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  10 SEEEEANYWKDLAMTYKQRaENTQEELREFQEGSRE------YEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFE 83
Cdd:COG5185  210 SETGNLGSESTLLEKAKEI-INIEEALKGFQDPESEledlaqTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLI 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  84 VQHSEGYRQISALEDDLAQTKAIkDQLQKYIRELEqANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL 163
Cdd:COG5185  289 KQFENTKEKIAEYTKSIDIKKAT-ESLEEQLAAAE-AEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENI 366
                        170
                 ....*....|....*.
gi 530408290 164 ESVQRLKDEARDLRQE 179
Cdd:COG5185  367 VGEVELSKSSEELDSF 382
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
19-202 4.87e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 38.93  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   19 KDLAMTYKQRAENTQEELR----EFQEGSREYE----------AELEtQLQQIETRNRDLLSENNrlrmELETIKEKFEV 84
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQLKiitmELQKKSSELEemtkfknnkeVELE-ELKKILAEDEKLLDEKK----QFEKIAEELKG 436
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   85 QHSEGYRQISALEDDL----AQTKAIKDQLQKYIRELEQANDDLERAKRATI--------MSLEDFE------------Q 140
Cdd:pfam05483 437 KEQELIFLLQAREKEIhdleIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIeltahcdkLLLENKEltqeasdmtlelK 516
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530408290  141 RLNQAIERNAFLESE-LDEKENLLESVQRLKDEARDLRQELavQQKQEKPRTPMPSSVEAERT 202
Cdd:pfam05483 517 KHQEDIINCKKQEERmLKQIENLEEKEMNLRDELESVREEF--IQKGDEVKCKLDKSEENARS 577
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
8-174 4.98e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 4.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   8 FSSEEEEANYWKDLAMTYKQ--RAENTQEELREFQEGSREYEAELETQLQQIETRNRDLlsenNRLRMELETIKEKF-EV 84
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL----EELRKELEELEKKYsEE 659
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  85 QHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRAtimsledfeqrLNQAIERNAFLESELDEKENLLE 164
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE-----------REKAKKELEKLEKALERVEELRE 728
                        170
                 ....*....|
gi 530408290 165 SVQRLKDEAR 174
Cdd:PRK03918 729 KVKKYKALLK 738
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
44-186 5.75e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 38.66  E-value: 5.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  44 REYEA--ELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEgyrqisaleddLAQTKAIKDQLQKYIRELEQAN 121
Cdd:PRK04778 300 REVKArkYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESE-----------LESVRQLEKQLESLEKQYDEIT 368
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530408290 122 DDLERAKRATIMSLEDFEQRLNQ--AIErnafleselDEKENLLESVQRLKDEARDLRQELAVQQKQ 186
Cdd:PRK04778 369 ERIAEQEIAYSELQEELEEILKQleEIE---------KEQEKLSEMLQGLRKDELEAREKLERYRNK 426
GrpE pfam01025
GrpE;
47-127 6.01e-03

GrpE;


Pssm-ID: 425996 [Multi-domain]  Cd Length: 165  Bit Score: 37.20  E-value: 6.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   47 EAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEvqhsegyRQISaleddlaqtKAIKDQLQKYIRELEQANDDLER 126
Cdd:pfam01025  13 IESLEEEIEELEKKIEELKEKLLRALAEFENLRKRTE-------KEKE---------EAKKFAIEKFAKDLLPVIDNLER 76

                  .
gi 530408290  127 A 127
Cdd:pfam01025  77 A 77
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
27-188 6.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  27 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKF-EVQHSEgyrqiSALEDDLAQTKA 105
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYlELKDAE-----KELEREEKELKK 623
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290 106 IKDQLQKYIRELEQANDDLERAKR-----ATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKeleelEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703

                 ....*...
gi 530408290 181 AVQQKQEK 188
Cdd:PRK03918 704 EEREKAKK 711
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
91-193 6.17e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.21  E-value: 6.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  91 RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllesvQRLK 170
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR------AELE 100
                         90       100
                 ....*....|....*....|...
gi 530408290 171 DEARDLRQELAVQQKQEKPRTPM 193
Cdd:COG4942  101 AQKEELAELLRALYRLGRQPPLA 123
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
26-181 6.90e-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: 6.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   26 KQRAENTQEELREFQEGSREYEAELET----------QLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGY--RQI 93
Cdd:COG4913   677 LERLDASSDDLAALEEQLEELEAELEEleeeldelkgEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeeRFA 756
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   94 SALEDDLAQT--KAIKDQLQKYIRELEQANDDLERAKR--------------ATIMSLEDFEQRLNQAIE---------- 147
Cdd:COG4913   757 AALGDAVERElrENLEERIDALRARLNRAEEELERAMRafnrewpaetadldADLESLPEYLALLDRLEEdglpeyeerf 836
                         170       180       190
                  ....*....|....*....|....*....|....
gi 530408290  148 RNAFLESELDEKENLLesvQRLKDEARDLRQELA 181
Cdd:COG4913   837 KELLNENSIEFVADLL---SKLRRAIREIKERID 867
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
24-186 7.88e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.10  E-value: 7.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  24 TYKQRAENTQEELREFQEGSREYEAELETQLQQIETRN-RDLLSENNRLRMELETIKEKFEVQHSEGYRQISALED---- 98
Cdd:PRK02224 166 EYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDlHERLNGLESELAELDEEIERYEEQREQARETRDEADEvlee 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  99 ------DLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDE 172
Cdd:PRK02224 246 heerreELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE 325
                        170
                 ....*....|....
gi 530408290 173 ARDLRQELAVQQKQ 186
Cdd:PRK02224 326 LRDRLEECRVAAQA 339
fliH PRK06669
flagellar assembly protein H; Validated
67-180 8.04e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 37.69  E-value: 8.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  67 ENNRLRMELETIKEKFEVQHSEGYRQIS--ALEDDLAQTKAIKDQLqkyIRELEQANDDLERAKRATIMSLE----DFEQ 140
Cdd:PRK06669  34 EKERLREEEEEQVEQLREEANDEAKEIIeeAEEDAFEIVEAAEEEA---KEELLKKTDEASSIIEKLQMQIEreqeEWEE 110
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530408290 141 RLNQAIER---NAFLESELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:PRK06669 111 ELERLIEEakaEGYEEGYEKGREEGLEEVRELIEQLNKIIEKL 153
Yuri_gagarin pfam15934
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
49-196 8.23e-03

Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.


Pssm-ID: 318204 [Multi-domain]  Cd Length: 234  Bit Score: 37.25  E-value: 8.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   49 ELETQLQQIETRNRDLlSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAK 128
Cdd:pfam15934  76 HQIKQLQSMITGYSDI-SENNRLKEEIHDLKQKNCVQARVVRKMGLELKGQEEQRVELCDKYESLLGSFEEQCQELKRAN 154
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  129 RatimSLEDFEQRLNQaIERnafLESELDEKENLL-ESVQRLKD-EARDLRQELAVQQKQEKPRTPMPSS 196
Cdd:pfam15934 155 R----RVQSLQTRLSQ-VEK---LQEELRTERKILrEEVIALKEkDAKSNGRERALQDQLKCCQTEIEKS 216
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
26-171 8.28e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 38.39  E-value: 8.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   26 KQRAENTQEELREFQEGSREYEAELE----------TQLQQ---IETRNRDLLSENNRLRMELETIKEKFEvQHSEGYRQ 92
Cdd:COG3096   305 QYRLVEMARELEELSARESDLEQDYQaasdhlnlvqTALRQqekIERYQEDLEELTERLEEQEEVVEEAAE-QLAEAEAR 383
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290   93 ISALEDDLaqtKAIKDQLQKYIRELE----------QANDDLERAKR---ATIMSLEDFEQRLNQAIERnaflESELDEK 159
Cdd:COG3096   384 LEAAEEEV---DSLKSQLADYQQALDvqqtraiqyqQAVQALEKARAlcgLPDLTPENAEDYLAAFRAK----EQQATEE 456
                         170
                  ....*....|..
gi 530408290  160 enLLESVQRLKD 171
Cdd:COG3096   457 --VLELEQKLSV 466
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
10-185 8.76e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 8.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  10 SEEEEanywKDLAMTYKQRAENTQEELREFQEGSREYEAE---LETQLQQIET--RNRDLLSENNRLRMELETI-KEKFE 83
Cdd:PRK03918 446 TEEHR----KELLEEYTAELKRIEKELKEIEEKERKLRKElreLEKVLKKESEliKLKELAEQLKELEEKLKKYnLEELE 521
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408290  84 vQHSEGYR-----------QISALEDDLAQTKAIKDQLQKYIRELEQANDDLE----RAKRATIMSLEDFE---QRLNQA 145
Cdd:PRK03918 522 -KKAEEYEklkekliklkgEIKSLKKELEKLEELKKKLAELEKKLDELEEELAellkELEELGFESVEELEerlKELEPF 600
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530408290 146 IERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:PRK03918 601 YNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
 
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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