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Conserved domains on  [gi|50290569|ref|XP_447716|]
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uncharacterized protein GVI51_I10747 [Nakaseomyces glabratus]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1003417)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG1340 super family cl34231
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
20-267 9.69e-11

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


The actual alignment was detected with superfamily member COG1340:

Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 62.62  E-value: 9.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  20 KKLETLNVQLKKIDEELNQLRKQIDQnqvndkTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGEIQ 99
Cdd:COG1340  29 EKRDELNEELKELAEKRDELNAQVKE------LREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELA 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569 100 DRIGKKskyTTTAEAKQRINQIEDQISTGDMSLVEEKMLVKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKLKEELSgm 179
Cdd:COG1340 103 ELNKAG---GSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAE-- 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569 180 nsrelsaqfdENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREEEE 259
Cdd:COG1340 178 ----------EIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247


                ....*...
gi 50290569 260 KLSKVLEE 267
Cdd:COG1340 248 KLRKKQRA 255
 
Name Accession Description Interval E-value
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
20-267 9.69e-11

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 62.62  E-value: 9.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  20 KKLETLNVQLKKIDEELNQLRKQIDQnqvndkTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGEIQ 99
Cdd:COG1340  29 EKRDELNEELKELAEKRDELNAQVKE------LREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELA 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569 100 DRIGKKskyTTTAEAKQRINQIEDQISTGDMSLVEEKMLVKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKLKEELSgm 179
Cdd:COG1340 103 ELNKAG---GSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAE-- 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569 180 nsrelsaqfdENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREEEE 259
Cdd:COG1340 178 ----------EIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247


                ....*...
gi 50290569 260 KLSKVLEE 267
Cdd:COG1340 248 KLRKKQRA 255
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 4-280 3.22e-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: 3.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569      4 QQQQQRIKRPDVSVRDKKLETLNVQLKKIDEELNQLRKQID-QNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHD 82
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569     83 SIKQLDSQIKRRTGEIQdrigkkskytttaEAKQRINQIEDQISTGDMSLVEEKMLVKELNS-----LNKLIKDLVAIDP 157
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIE-------------ELEAQIEQLKEELKALREALDELRAELTLLNEeaanlRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569    158 IKKAIDTDKDKIVKLKEELSgmnsrELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIradf 237
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIE-----SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL---- 906

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 50290569    238 DNEFKAFKNKLEKqrlKREEEEKLSKVLEEKDAKLGKLQEKLT 280
Cdd:TIGR02168  907 ESKRSELRRELEE---LREKLAQLELRLEGLEVRIDNLQERLS 946
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 19-136 5.57e-05

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 44.98  E-value: 5.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569    19 DKKLETLNVQLKKIDEELNQLRKQIDQNQVNDKTQNERKKlQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGEI 98
Cdd:pfam03961 155 KEKLEELEKELEELEEELEKLKKRLKKLPKKARGQLPPEK-REQLEKLLETKNKLSEELEELEEELKELKEELESLLGEG 233

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 50290569    99 QDRIGKKSKYTTTAEAKQRINQIEDQISTGDMSLVEEK 136
Cdd:pfam03961 234 KISVNKTIYPGVTIQIGNKTLRIKREYGPCTFVFEDGE 271
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
19-277 1.21e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569   19 DKKLETLNVQLKKIDEELNQLRKQIDQNQVNDKTQNERKKLQEKTKEIIKTQAD----LKARRNAIHDSIKQLDSQIKRR 94
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEeyekLKEKLIKLKGEIKSLKKELEKL 551

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569   95 TGEIQDRIGKKSKyttTAEAKQRINQIEDQISTGDMSLVEEkmLVKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKLKE 174
Cdd:PRK03918 552 EELKKKLAELEKK---LDELEEELAELLKELEELGFESVEE--LEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  175 ELSGM--NSRELSAQFDENQKRLNELQSS-TQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQ 251
Cdd:PRK03918 627 ELDKAfeELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706

                        250       260
                 ....*....|....*....|....*.
gi 50290569  252 RLKREEEEKLSKVLEEKDAKLGKLQE 277
Cdd:PRK03918 707 EKAKKELEKLEKALERVEELREKVKK 732
 
Name Accession Description Interval E-value
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
20-267 9.69e-11

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 62.62  E-value: 9.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  20 KKLETLNVQLKKIDEELNQLRKQIDQnqvndkTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGEIQ 99
Cdd:COG1340  29 EKRDELNEELKELAEKRDELNAQVKE------LREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELA 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569 100 DRIGKKskyTTTAEAKQRINQIEDQISTGDMSLVEEKMLVKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKLKEELSgm 179
Cdd:COG1340 103 ELNKAG---GSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAE-- 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569 180 nsrelsaqfdENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREEEE 259
Cdd:COG1340 178 ----------EIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247


                ....*...
gi 50290569 260 KLSKVLEE 267
Cdd:COG1340 248 KLRKKQRA 255
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 45-283 2.55e-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: 49.38  E-value: 2.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  45 QNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGEIQdrigkkskytttaEAKQRINQIEDQ 124
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-------------ALEQELAALEAE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569 125 ISTGDMslvEEKMLVKELNSLNKLIKDLVAIdpIKKAIDTDKDKIVKLKEELSGMNSRE--LSAQFDENQKRLNELQSST 202
Cdd:COG4942  85 LAELEK---EIAELRAELEAQKEELAELLRA--LYRLGRQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569 203 QTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREEEEKLSKVLEEKDAKLGKLQEKLTHA 282
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239


                .
gi 50290569 283 R 283
Cdd:COG4942 240 A 240
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 4-280 3.22e-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: 3.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569      4 QQQQQRIKRPDVSVRDKKLETLNVQLKKIDEELNQLRKQID-QNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHD 82
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569     83 SIKQLDSQIKRRTGEIQdrigkkskytttaEAKQRINQIEDQISTGDMSLVEEKMLVKELNS-----LNKLIKDLVAIDP 157
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIE-------------ELEAQIEQLKEELKALREALDELRAELTLLNEeaanlRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569    158 IKKAIDTDKDKIVKLKEELSgmnsrELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIradf 237
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIE-----SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL---- 906

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 50290569    238 DNEFKAFKNKLEKqrlKREEEEKLSKVLEEKDAKLGKLQEKLT 280
Cdd:TIGR02168  907 ESKRSELRRELEE---LREKLAQLELRLEGLEVRIDNLQERLS 946
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 18-283 1.20e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 1.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  18 RDKKLETLNVQLKKIDEELNQLRKQIDQNQVndKTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGE 97
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEA--ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  98 IQDRIGKKSKyttTAEAKQRINQIEDQISTgdmSLVEEKMLVKELNSLNKLIKDLvaidpiKKAIDTDKDKIVKLKEELS 177
Cdd:COG1196 315 EERLEELEEE---LAELEEELEELEEELEE---LEEELEEAEEELEEAEAELAEA------EEALLEAEAELAEAEEELE 382

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569 178 GMNSRELSAQFDENQKRLNELQSSTQtvfdkRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREE 257
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEA-----EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                       250       260
                ....*....|....*....|....*.
gi 50290569 258 EEKLSKVLEEKDAKLGKLQEKLTHAR 283
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELL 483
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 20-307 2.89e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569     20 KKLETLNVQLKKIDEELNQLRKQIDqnqvNDKTQNER-KKLQEKTKEIIKTQADLKARRnaihdsIKQLDSQIKRRTGEI 98
Cdd:TIGR02168  179 RKLERTRENLDRLEDILNELERQLK----SLERQAEKaERYKELKAELRELELALLVLR------LEELREELEELQEEL 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569     99 QDRIGKKSKYTTTAEAKQ-RINQIEDQISTGDMSLVEekmLVKELNSLNKLIKDLVA-IDPIKKAIDTDKDKIVKLKEEL 176
Cdd:TIGR02168  249 KEAEEELEELTAELQELEeKLEELRLEVSELEEEIEE---LQKELYALANEISRLEQqKQILRERLANLERQLEELEAQL 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569    177 sgmnsRELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKRE 256
Cdd:TIGR02168  326 -----EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 50290569    257 EEEKLSKVLEEKDAKLGKLQEKLTHARIPAFTYEIEAIENTLVILDPTFEK 307
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 16-232 3.04e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 3.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569     16 SVRDKKLETLNVQLKKIDEELNQLRKQIDQ-----NQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQ---L 87
Cdd:TIGR02169  787 RLSHSRIPEIQAELSKLEEEVSRIEARLREieqklNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKkeeL 866

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569     88 DSQIKRRTGEIQDRIGKKSKYTTT--------AEAKQRINQIEDQISTGD--MSLVEEKM--LVKELNSLNKLIKDLVAI 155
Cdd:TIGR02169  867 EEELEELEAALRDLESRLGDLKKErdeleaqlRELERKIEELEAQIEKKRkrLSELKAKLeaLEEELSEIEDPKGEDEEI 946

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50290569    156 DPIKKAIDTDKDKIVKLKEELSGMNSRELSA--QFDENQKRLNELQsstqtvfDKRQTLYNKRTALyKKRDEVYSQIRK 232
Cdd:TIGR02169  947 PEEELSLEDVQAELQRVEEEIRALEPVNMLAiqEYEEVLKRLDELK-------EKRAKLEEERKAI-LERIEEYEKKKR 1017
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 19-136 5.57e-05

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 44.98  E-value: 5.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569    19 DKKLETLNVQLKKIDEELNQLRKQIDQNQVNDKTQNERKKlQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGEI 98
Cdd:pfam03961 155 KEKLEELEKELEELEEELEKLKKRLKKLPKKARGQLPPEK-REQLEKLLETKNKLSEELEELEEELKELKEELESLLGEG 233

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 50290569    99 QDRIGKKSKYTTTAEAKQRINQIEDQISTGDMSLVEEK 136
Cdd:pfam03961 234 KISVNKTIYPGVTIQIGNKTLRIKREYGPCTFVFEDGE 271
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
56-283 9.94e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 9.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569   56 RKKLQEKTKEIiktqADLKARRNAIHDSIKQLDSQIKRRTgEIQDRIGKKSKYT----TTAEAKQRINQIEDQI-----S 126
Cdd:COG4913  609 RAKLAALEAEL----AELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSwdeiDVASAEREIAELEAELerldaS 683

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  127 TGDMSLVEEKM--LVKELNSLNKLIKDL-VAIDPIKKAIDTDKDKIVKLKEELSGMNSRELSAQFDENQKRLNELQsSTQ 203
Cdd:COG4913  684 SDDLAALEEQLeeLEAELEELEEELDELkGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL-GDA 762

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  204 TVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFK-----------------NKLEKQRLKREEEEKLSKVLE 266
Cdd:COG4913  763 VERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETadldadleslpeylallDRLEEDGLPEYEERFKELLNE 842

                        250
                 ....*....|....*..
gi 50290569  267 EKDAKLGKLQEKLTHAR 283
Cdd:COG4913  843 NSIEFVADLLSKLRRAI 859
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
19-277 1.21e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569   19 DKKLETLNVQLKKIDEELNQLRKQIDQNQVNDKTQNERKKLQEKTKEIIKTQAD----LKARRNAIHDSIKQLDSQIKRR 94
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEeyekLKEKLIKLKGEIKSLKKELEKL 551

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569   95 TGEIQDRIGKKSKyttTAEAKQRINQIEDQISTGDMSLVEEkmLVKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKLKE 174
Cdd:PRK03918 552 EELKKKLAELEKK---LDELEEELAELLKELEELGFESVEE--LEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  175 ELSGM--NSRELSAQFDENQKRLNELQSS-TQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQ 251
Cdd:PRK03918 627 ELDKAfeELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706

                        250       260
                 ....*....|....*....|....*.
gi 50290569  252 RLKREEEEKLSKVLEEKDAKLGKLQE 277
Cdd:PRK03918 707 EKAKKELEKLEKALERVEELREKVKK 732
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 21-279 1.88e-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: 44.29  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569     21 KLETLNVQLKKIDEELNQLRKQID-QNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGEIQ 99
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRrIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569    100 DRIGKKSKYTTTAEAKQR-INQIEDQISTGDMSLVEEKmlvkelnslnklikdlvaidpikkaIDTDKDKIVKLKEELSg 178
Cdd:TIGR02169  755 NVKSELKELEARIEELEEdLHKLEEALNDLEARLSHSR-------------------------IPEIQAELSKLEEEVS- 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569    179 mnsrELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREEE 258
Cdd:TIGR02169  809 ----RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884

                          250       260
                   ....*....|....*....|.
gi 50290569    259 EKLSKVLEEKDAKLGKLQEKL 279
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKI 905
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 7-222 2.92e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 2.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569   7 QQRIKRPDVSVRDKKLETLNVQLKKIDEELNQLRKQIdqNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQ 86
Cdd:COG3883  17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEY--NELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  87 LdsqikRRTGEIQDRIGKKSKYTTTAEAKQRINQIeDQISTGDMSLVEEkmlvkelnslnkLIKDLVAIDPIKKAIDTDK 166
Cdd:COG3883  95 L-----YRSGGSVSYLDVLLGSESFSDFLDRLSAL-SKIADADADLLEE------------LKADKAELEAKKAELEAKL 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 50290569 167 DKIVKLKEELSGMnSRELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKK 222
Cdd:COG3883 157 AELEALKAELEAA-KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-283 3.64e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 3.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569      3 SQQQQQRIKRPDVSVRDKKLETLNVQLKKIDEELNQLrkqidqnqvndktqneRKKLQEKTKEIiktqADLKARRNAIHD 82
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL----------------QKELYALANEI----SRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569     83 SIKQLDSQIKRRTGEIQDrigKKSKYTTTAEAKQRINQIEDQIstgdmsLVEEKMLVKELNSLNKLIKDLV-AIDPIKKA 161
Cdd:TIGR02168  310 RLANLERQLEELEAQLEE---LESKLDELAEELAELEEKLEEL------KEELESLEAELEELEAELEELEsRLEELEEQ 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569    162 IDTDKDKIVKLKEELsgmnsRELSAQFDENQKRLNELQsstqtvfDKRQTLYNKRTALYKKRDEvySQIRKIRADFDNEF 241
Cdd:TIGR02168  381 LETLRSKVAQLELQI-----ASLNNEIERLEARLERLE-------DRRERLQQEIEELLKKLEE--AELKELQAELEELE 446

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 50290569    242 KAFKNKLEKQRLKREEEEKLSKVLEEKDAKLGKLQEKLTHAR 283
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 21-452 5.55e-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: 5.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569     21 KLETLNVQLKKIDEELNQLRKQIdqNQVNDKTQNERKKLQEKTKEIiktqADLKARRNAIHDSIKQLDSQIKRRTGEIQD 100
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEV--SELEEEIEELQKELYALANEI----SRLEQQKQILRERLANLERQLEELEAQLEE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569    101 rigKKSKYTTTAEAKQRINQIEDQIstgdmsLVEEKMLVKELNSLNKLIKDLV-AIDPIKKAIDTDKDKIVKLKEELSGM 179
Cdd:TIGR02168  328 ---LESKLDELAEELAELEEKLEEL------KEELESLEAELEELEAELEELEsRLEELEEQLETLRSKVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569    180 NSR--ELSAQFDENQKRLNELQSSTQTVFDKRQTlyNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREE 257
Cdd:TIGR02168  399 NNEieRLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569    258 EEKLSKVLEEKDAKLGKLQEKLTHARipAFTYEIEAIEN-------------TLVILDPTFEKPKKNVLQElenGAAEPV 324
Cdd:TIGR02168  477 LDAAERELAQLQARLDSLERLQENLE--GFSEGVKALLKnqsglsgilgvlsELISVDEGYEAAIEAALGG---RLQAVV 551

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569    325 MSNAPVNNDGLVLVEKKDDS------YNRVAPSKSKKHKKKSQSAKEPSSQNLFTKVDGKITLEPTLIATLAELDVTvpi 398
Cdd:TIGR02168  552 VENLNAAKKAIAFLKQNELGrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVV--- 628

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50290569    399 tqDDVATSVEQLKKKLEEF----------------------KSNQDEQTEKNIKAVEEQMKKLELAYEEKENEVKR 452
Cdd:TIGR02168  629 --DDLDNALELAKKLRPGYrivtldgdlvrpggvitggsakTNSSILERRREIEELEEKIEELEEKIAELEKALAE 702
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 33-245 7.16e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 42.35  E-value: 7.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569     33 DEELNQLRKQIDQNQVNDKTQNERKKLQEKTKEIIKT-QADLKARRNAIHD-SIKQLDSQIKRRTGEIQDRIGK-KSKYT 109
Cdd:TIGR01612 1482 DFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQyKKDVTELLNKYSAlAIKNKFAKTKKDSEIIIKEIKDaHKKFI 1561

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569    110 TTAE-AKQRINQI-------EDQISTGDMSlveEKMLVKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKLKEELSGMNS 181
Cdd:TIGR01612 1562 LEAEkSEQKIKEIkkekfriEDDAAKNDKS---NKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSI 1638

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50290569    182 RELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALykkrDEVYSQIRKIRADFDNEFKAFK 245
Cdd:TIGR01612 1639 DSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKEL----DELDSEIEKIEIDVDQHKKNYE 1698
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
19-199 1.06e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 1.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  19 DKKLETLNVQLKKIDEELNQLRKQIDQNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIhdsikqldSQIKRRTGEI 98
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL--------AALRAQLGSG 252

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  99 QDRIGKKSKYTTTAEAKQRINQIEDQISTGDMSLVEE----KMLVKELNSLNKLIKDLVA--IDPIKKAIDTDKDKIVKL 172
Cdd:COG3206 253 PDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQLQQEAQriLASLEAELEALQAREASL 332

                       170       180
                ....*....|....*....|....*..
gi 50290569 173 KEELSGMNSRelSAQFDENQKRLNELQ 199
Cdd:COG3206 333 QAQLAQLEAR--LAELPELEAELRRLE 357
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 28-275 1.17e-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: 41.29  E-value: 1.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  28 QLKKIDEELNQLRKQIDQNQvndktqnerKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDsQIKRRTGEIQDRIGKKSK 107
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELE---------KELAALKKEEKALLKQLAALERRIAALARRIR-ALEQELAALEAELAELEK 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569 108 YTTTAEA--KQRINQIEDQISTG-DMSLVEEKMLVKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKLKEELsgmnsREL 184
Cdd:COG4942  91 EIAELRAelEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL-----AAL 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569 185 SAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREEEEKLSKV 264
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245

                       250
                ....*....|.
gi 50290569 265 LEEKDAKlGKL 275
Cdd:COG4942 246 AGFAALK-GKL 255
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
18-262 1.48e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569   18 RDKKLETLNVQLKKIDEELNQLRKQIDQNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGE 97
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569   98 IQDrigkksKYTTTAEAKQRINQIEDQISTGDMSLVEEKmlvKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKL----- 172
Cdd:PRK02224 553 AEE------KREAAAEAEEEAEEAREEVAELNSKLAELK---ERIESLERIRTLLAAIADAEDEIERLREKREALaelnd 623

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  173 --KEELSGMNSR--ELSAQFDENqkRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDN------EFK 242
Cdd:PRK02224 624 erRERLAEKRERkrELEAEFDEA--RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEleelreRRE 701

                        250       260
                 ....*....|....*....|
gi 50290569  243 AFKNKLEKQRLKREEEEKLS 262
Cdd:PRK02224 702 ALENRVEALEALYDEAEELE 721
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 19-270 1.98e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569     19 DKKLETLNVQLKKIDEELNQLRKQIDQNqvNDKTQNERKKLQEKTKEIIK----TQADLKARRNAIHDSIKQLDSQIKRR 94
Cdd:TIGR02169  236 ERQKEAIERQLASLEEELEKLTEEISEL--EKRLEEIEQLLEELNKKIKDlgeeEQLRVKEKIGELEAEIASLERSIAEK 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569     95 TGEIQDRIGKKskytttAEAKQRINQIEDQISTGDMSLVEEKM----LVKELNSLNKLIKDLVA-IDPIKKAIDTDKDKI 169
Cdd:TIGR02169  314 ERELEDAEERL------AKLEAEIDKLLAEIEELEREIEEERKrrdkLTEEYAELKEELEDLRAeLEEVDKEFAETRDEL 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569    170 VKLKEELSGMNS------RELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVY------SQIRKIRADF 237
Cdd:TIGR02169  388 KDYREKLEKLKReinelkRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKkqewklEQLAADLSKY 467

                          250       260       270
                   ....*....|....*....|....*....|....
gi 50290569    238 DNEFKAFKNKLEK-QRLKREEEEKLSKVLEEKDA 270
Cdd:TIGR02169  468 EQELYDLKEEYDRvEKELSKLQRELAEAEAQARA 501
46 PHA02562
endonuclease subunit; Provisional
 21-281 1.99e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569   21 KLETLNVQLKKIDEELNQLRKQID-----QNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRT 95
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKtynknIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPS 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569   96 GEIQDrigkkskytttaeakqrINQIEDQIstgdmslveeKMLVKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKLKEE 175
Cdd:PHA02562 255 AALNK-----------------LNTAAAKI----------KSKIEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDK 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  176 LSGMNS--RELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDevysQIRKIRADFDnefkafknKLEKQRL 253
Cdd:PHA02562 308 LKELQHslEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVD----KAKKVKAAIE--------ELQAEFV 375

                        250       260
                 ....*....|....*....|....*....
gi 50290569  254 KREEE-EKLSKVLEEKDAKLGKLQEKLTH 281
Cdd:PHA02562 376 DNAEElAKLQDELDKIVKTKSELVKEKYH 404
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 20-200 2.01e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 2.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  20 KKLETLnVQLKKIDEELNQLRKQidqnqvndktqneRKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGEIQ 99
Cdd:COG1579   4 EDLRAL-LDLQELDSELDRLEHR-------------LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569 100 drigkkskytttaEAKQRINQIEDQISTGdMSLVEEKMLVKELNSLNKLIKDL--------VAIDPIKKAIDTDKDKIVK 171
Cdd:COG1579  70 -------------EVEARIKKYEEQLGNV-RNNKEYEALQKEIESLKRRISDLedeilelmERIEELEEELAELEAELAE 135

                       170       180
                ....*....|....*....|....*....
gi 50290569 172 LKEELSGMnSRELSAQFDENQKRLNELQS 200
Cdd:COG1579 136 LEAELEEK-KAELDEELAELEAELEELEA 163
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
50-278 4.58e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 4.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569   50 DKTQNERKKLQEKTKEIiktqadlKARRNAIHDSIKqldsqikrRTGEIQDRIGKKSKYTTtaEAKQRINQIEDQISTGD 129
Cdd:PRK03918 158 DDYENAYKNLGEVIKEI-------KRRIERLEKFIK--------RTENIEELIKEKEKELE--EVLREINEISSELPELR 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  130 MSLVEEKMLVKELNSLNKLIKDL-VAIDPIKKAIDTDKDKIVKLKEELSGmnSRELSAQFDENQKRLNELQsstqtvfdK 208
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEIEELeKELESLEGSKRKLEEKIRELEERIEE--LKKEIEELEEKVKELKELK--------E 290

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  209 RQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREEEEKLSKVLEEKDAKLGKLQEK 278
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360
PRK01156 PRK01156
chromosome segregation protein; Provisional
 29-148 6.16e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.11  E-value: 6.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569   29 LKKIDEELNQLRKQIDQNQVND-------KTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRrtgEIQDR 101
Cdd:PRK01156 621 IREIENEANNLNNKYNEIQENKilieklrGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDD---AKANR 697

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 50290569  102 IGKKSKYTTTaeaKQRINQIEDQISTGDMSLVEEKMLVKELNSLNKL 148
Cdd:PRK01156 698 ARLESTIEIL---RTRINELSDRINDINETLESMKKIKKAIGDLKRL 741
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 5-248 6.67e-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: 38.59  E-value: 6.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569   5 QQQQRIKRPDVSVRDKKLETLNVQLKKIDEELNQLRKQIdqNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHDSI 84
Cdd:COG4942  33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI--RALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  85 KQLdsQIKRRTGEIQDRIGKKSkytttAEAKQRINQIEDQISTGDMSLVEEkmlvkelnslnkLIKDLVAIDPIKKAIDT 164
Cdd:COG4942 111 RAL--YRLGRQPPLALLLSPED-----FLDAVRRLQYLKYLAPARREQAEE------------LRADLAELAALRAELEA 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569 165 DKDKIVKLKEELSGmNSRELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNE-FKA 243
Cdd:COG4942 172 ERAELEALLAELEE-ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAgFAA 250


                ....*
gi 50290569 244 FKNKL 248
Cdd:COG4942 251 LKGKL 255
PRK12704 PRK12704
phosphodiesterase; Provisional
 132-281 6.80e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 6.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  132 LVEEKMLVKELNSLNKLIKDLVAiDPIKKAIDTDKDKIVKLKEELSgmnsrELSAQFD-ENQKRLNELQSSTQTVFDKRQ 210
Cdd:PRK12704  23 FVRKKIAEAKIKEAEEEAKRILE-EAKKEAEAIKKEALLEAKEEIH-----KLRNEFEkELRERRNELQKLEKRLLQKEE 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50290569  211 TLyNKRTALYKKRDEvysQIRKIRADFDNEFKAFKNKLEK-QRLKREEEEKLSKV--LEEKDAK---LGKLQEKLTH 281
Cdd:PRK12704  97 NL-DRKLELLEKREE---ELEKKEKELEQKQQELEKKEEElEELIEEQLQELERIsgLTAEEAKeilLEKVEEEARH 169
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
90-280 9.35e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 9.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569   90 QIK--RRTGEIQDRIGKKSKYTTTAEAKQRINQIEDQISTGDMSLVEEKMLVKELNS-LNKLIKDLVAIDPIKKAIDTDK 166
Cdd:COG4913  582 QVKgnGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAeLDALQERREALQRLAEYSWDEI 661

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50290569  167 D------KIVKLKEELSGMNS-----RELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKI-- 233
Cdd:COG4913  662 DvasaerEIAELEAELERLDAssddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAed 741

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 50290569  234 ------RADFDNEFKAfknkLEKQRLKREEEEKLSKVLEEKDAKLGKLQEKLT 280
Cdd:COG4913  742 larlelRALLEERFAA----ALGDAVERELRENLEERIDALRARLNRAEEELE 790
 
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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