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Conserved domains on  [gi|767999315|ref|XP_011524504|]
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coiled-coil domain-containing protein 68 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
120-291 9.78e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 9.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315   120 REAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLlQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQITELENLVQRME 199
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKEAEEELEEL-TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315   200 KEKRTLLERKLSLENKLLQLK-SSATYGKSCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRI 278
Cdd:TIGR02168  302 QQKQILRERLANLERQLEELEaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
                          170
                   ....*....|...
gi 767999315   279 ENLREKVNILEAQ 291
Cdd:TIGR02168  382 ETLRSKVAQLELQ 394
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
120-291 9.78e-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: 46.97  E-value: 9.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315   120 REAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLlQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQITELENLVQRME 199
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKEAEEELEEL-TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315   200 KEKRTLLERKLSLENKLLQLK-SSATYGKSCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRI 278
Cdd:TIGR02168  302 QQKQILRERLANLERQLEELEaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
                          170
                   ....*....|...
gi 767999315   279 ENLREKVNILEAQ 291
Cdd:TIGR02168  382 ETLRSKVAQLELQ 394
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
88-291 1.08e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315  88 LDLLMKKIKGKDLQLLEMNKENEVLKIKLQASREAGAAALRnvAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKL 167
Cdd:COG1196  248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQA--EEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315 168 KQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQ-LKSSATYGKSCQDLQREISILQEQISHL 246
Cdd:COG1196  326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEaEEELEELAEELLEALRAAAELAAQLEEL 405
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767999315 247 QFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQ 291
Cdd:COG1196  406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
110-288 8.90e-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: 40.65  E-value: 8.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315  110 EVLKIKLQASREAgaaalRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQIT 189
Cdd:pfam07888  30 ELLQNRLEECLQE-----RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315  190 ELENLVQRMEKEKRTLLERKLSLENKLLQLKS-SATYGKSCQDLQREISILQEQI--------------SHLQFVIHSQH 254
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRELEEdIKTLTQRVLERETELERMKERAkkagaqrkeeeaerKQLQAKLQQTE 184
                         170       180       190
                  ....*....|....*....|....*....|....
gi 767999315  255 QNLRSVIQEMEGLKNNLKEQDKRIENLREKVNIL 288
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTL 218
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
140-291 1.15e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 40.30  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315 140 TQSEEVRKKQEDSKQLLQVNKLEKeqkLKQHVE-NLNQVAEKLEEKHSQITELENLVQRMEKEKRtLLE--RKLSLENKL 216
Cdd:PRK05771  63 RSYLPKLNPLREEKKKVSVKSLEE---LIKDVEeELEKIEKEIKELEEEISELENEIKELEQEIE-RLEpwGNFDLDLSL 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315 217 LQLKSSATYGKSCQDLQREISILQEQISHLQFVIH--------------SQHQNLRSVIQEMEGLKNNLKEQ---DKRIE 279
Cdd:PRK05771 139 LLGFKYVSVFVGTVPEDKLEELKLESDVENVEYIStdkgyvyvvvvvlkELSDEVEEELKKLGFERLELEEEgtpSELIR 218
                        170
                 ....*....|..
gi 767999315 280 NLREKVNILEAQ 291
Cdd:PRK05771 219 EIKEELEEIEKE 230
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
120-291 9.78e-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: 46.97  E-value: 9.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315   120 REAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLlQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQITELENLVQRME 199
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKEAEEELEEL-TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315   200 KEKRTLLERKLSLENKLLQLK-SSATYGKSCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRI 278
Cdd:TIGR02168  302 QQKQILRERLANLERQLEELEaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
                          170
                   ....*....|...
gi 767999315   279 ENLREKVNILEAQ 291
Cdd:TIGR02168  382 ETLRSKVAQLELQ 394
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
94-291 1.01e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315    94 KIKGKDLQLLEMNKENEVLKiKLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLlQVNKLEKEQKLKQHVEN 173
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELE-EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL-EAQLEELESKLDELAEE 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315   174 LNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKS-SATYGKSCQDLQREISILQEQISHLQFVIHS 252
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQLELQIASLNNEIERLEARLERLEDRRER 418
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 767999315   253 QHQNLRSVIQ-----EMEGLKNNLKEQDKRIENLREKVNILEAQ 291
Cdd:TIGR02168  419 LQQEIEELLKkleeaELKELQAELEELEEELEELQEELERLEEA 462
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
88-291 1.08e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315  88 LDLLMKKIKGKDLQLLEMNKENEVLKIKLQASREAGAAALRnvAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKL 167
Cdd:COG1196  248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQA--EEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315 168 KQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQ-LKSSATYGKSCQDLQREISILQEQISHL 246
Cdd:COG1196  326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEaEEELEELAEELLEALRAAAELAAQLEEL 405
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767999315 247 QFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQ 291
Cdd:COG1196  406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
88-291 3.00e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 3.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315  88 LDLLMKKIKGKDLQLLEMNKENEVLKIKLQAsREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLlqvnklekEQKL 167
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEEAQAEEYELLAELARL--------EQDI 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315 168 KQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSAtygkscQDLQREISILQEQISHLQ 247
Cdd:COG1196  305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL------AEAEEALLEAEAELAEAE 378
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767999315 248 FVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQ 291
Cdd:COG1196  379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
87-291 3.88e-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: 3.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315    87 SLDLLMKKIKGKDLQLLEMNKENEVLKIKLQASREAGAAALRNVAQRLFEnyQTQSEEVRKKQEDSKQLLQVNKLEKEQK 166
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE--LTELEAEIEELEERLEEAEEELAEAEAE 783
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315   167 LKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKssatygKSCQDLQREISILQEQISHL 246
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE------RRLEDLEEQIEELSEDIESL 857
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 767999315   247 QFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQ 291
Cdd:TIGR02168  858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
150-285 1.21e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.31  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315 150 EDSKQLLQVNKLEKEQKLKQHVE-NLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSAtygKS 228
Cdd:COG2433  383 EELIEKELPEEEPEAEREKEHEErELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE---RR 459
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767999315 229 CQDLQREISILQEQIShlqfvihsqhqNLRSVIQEMEGLKNNLKEQDKRIENLREKV 285
Cdd:COG2433  460 EIRKDREISRLDREIE-----------RLERELEEERERIEELKRKLERLKELWKLE 505
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
117-287 2.67e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315  117 QASREAGAAALRNVAQRLFEnyQTQSEEVRKKQEDSKQLLQVNKLEKEQkLKQHVENLNQVAEKLEEKHSQ-----ITEL 191
Cdd:COG4913   267 ARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELER-LEARLDALREELDELEAQIRGnggdrLEQL 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315  192 ENLVQRMEKEKRTLLERKLSLENKLLQLKSSATYGKscQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNL 271
Cdd:COG4913   344 EREIERLERELEERERRRARLEALLAALGLPLPASA--EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
                         170
                  ....*....|....*..
gi 767999315  272 KEQDKRIENLRE-KVNI 287
Cdd:COG4913   422 RELEAEIASLERrKSNI 438
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
116-288 6.82e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 6.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315 116 LQASREAGAAALRNVAQRLfENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKlkQHVENLNQVAEKLEEKHSQITELENLV 195
Cdd:COG3206  166 LELRREEARKALEFLEEQL-PELRKELEEAEAALEEFRQKNGLVDLSEEAK--LLLQQLSELESQLAEARAELAEAEARL 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315 196 QRMEKEKRT----------------LLERKLSLENKLLQLksSATYGK---SCQDLQREISILQEQISHLQFVIhsqhqn 256
Cdd:COG3206  243 AALRAQLGSgpdalpellqspviqqLRAQLAELEAELAEL--SARYTPnhpDVIALRAQIAALRAQLQQEAQRI------ 314
                        170       180       190
                 ....*....|....*....|....*....|..
gi 767999315 257 LRSVIQEMEGLKNNLKEQDKRIENLREKVNIL 288
Cdd:COG3206  315 LASLEAELEALQAREASLQAQLAQLEARLAEL 346
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
115-284 7.40e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 7.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315 115 KLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQITELENL 194
Cdd:COG1196  217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315 195 VQRMEKEKRTLLERKLSLENKLLQLKSS-ATYGKSCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKE 273
Cdd:COG1196  297 LARLEQDIARLEERRRELEERLEELEEElAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
                        170
                 ....*....|.
gi 767999315 274 QDKRIENLREK 284
Cdd:COG1196  377 AEEELEELAEE 387
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
110-288 8.90e-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: 40.65  E-value: 8.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315  110 EVLKIKLQASREAgaaalRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQIT 189
Cdd:pfam07888  30 ELLQNRLEECLQE-----RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315  190 ELENLVQRMEKEKRTLLERKLSLENKLLQLKS-SATYGKSCQDLQREISILQEQI--------------SHLQFVIHSQH 254
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRELEEdIKTLTQRVLERETELERMKERAkkagaqrkeeeaerKQLQAKLQQTE 184
                         170       180       190
                  ....*....|....*....|....*....|....
gi 767999315  255 QNLRSVIQEMEGLKNNLKEQDKRIENLREKVNIL 288
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTL 218
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
140-291 1.15e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 40.30  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315 140 TQSEEVRKKQEDSKQLLQVNKLEKeqkLKQHVE-NLNQVAEKLEEKHSQITELENLVQRMEKEKRtLLE--RKLSLENKL 216
Cdd:PRK05771  63 RSYLPKLNPLREEKKKVSVKSLEE---LIKDVEeELEKIEKEIKELEEEISELENEIKELEQEIE-RLEpwGNFDLDLSL 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315 217 LQLKSSATYGKSCQDLQREISILQEQISHLQFVIH--------------SQHQNLRSVIQEMEGLKNNLKEQ---DKRIE 279
Cdd:PRK05771 139 LLGFKYVSVFVGTVPEDKLEELKLESDVENVEYIStdkgyvyvvvvvlkELSDEVEEELKKLGFERLELEEEgtpSELIR 218
                        170
                 ....*....|..
gi 767999315 280 NLREKVNILEAQ 291
Cdd:PRK05771 219 EIKEELEEIEKE 230
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
178-291 1.67e-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: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315  178 AEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSATYGKSCQD---LQREISILQEQISHLQfvihSQH 254
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasAEREIAELEAELERLD----ASS 684
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767999315  255 QNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQ 291
Cdd:COG4913   685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
137-279 4.21e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.51  E-value: 4.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315   137 NYQTQSEEVRKKQEDSKQLlqVNKLEKEQKLKQHVEN-LNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENK 215
Cdd:TIGR02169  668 FSRSEPAELQRLRERLEGL--KRELSSLQSELRRIENrLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767999315   216 LLQLKSSATYGKS-CQDLQREISILQEQISHLQFVIHSQHQNL-RSVIQEMEGLKNNLKEQDKRIE 279
Cdd:TIGR02169  746 LSSLEQEIENVKSeLKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIE 811
PRK12704 PRK12704
phosphodiesterase; Provisional
90-218 4.75e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 4.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315  90 LLMKKIKGKDLQllemNKENEVLKIKLQASREAGAA---ALRNvAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQK 166
Cdd:PRK12704  23 FVRKKIAEAKIK----EAEEEAKRILEEAKKEAEAIkkeALLE-AKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEN 97
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767999315 167 LKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEkrtlLERKLSLENKLLQ 218
Cdd:PRK12704  98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEE----LEELIEEQLQELE 145
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
113-285 8.51e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.59  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315  113 KIKLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKE-QKLKQHVENLNQVAEKLEEKHS----- 186
Cdd:COG4913   611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDASSDdlaal 690
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315  187 --QITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSAtygKSCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEM 264
Cdd:COG4913   691 eeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL---DELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
                         170       180
                  ....*....|....*....|..
gi 767999315  265 -EGLKNNLKEQDKRIENLREKV 285
Cdd:COG4913   768 rENLEERIDALRARLNRAEEEL 789
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
101-291 8.96e-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: 37.74  E-value: 8.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315   101 QLLEMNKENEVLKIKLQASREAGAAALRNVAQRLfENYQTQSEEVRKKQEDSKQLLQvnklEKEQKLKQHVENLNQVAEK 180
Cdd:TIGR02169  319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRR-DKLTEEYAELKEELEDLRAELE----EVDKEFAETRDELKDYREK 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315   181 LEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSATygkscqDLQREISILQEQISHLQFVIHSQHQNLRSV 260
Cdd:TIGR02169  394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN------ELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
                          170       180       190
                   ....*....|....*....|....*....|.
gi 767999315   261 IQEMEGLKNNLKEQDKRIENLREKVNILEAQ 291
Cdd:TIGR02169  468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
88-277 9.20e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 37.44  E-value: 9.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315  88 LDLLMKKIKGKDLQLLEMNKENEVL----------KIKLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQL-L 156
Cdd:COG4717   44 RAMLLERLEKEADELFKPQGRKPELnlkelkeleeELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLeK 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767999315 157 QVNKLEKEQKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLksSATYGKSCQDLQREI 236
Cdd:COG4717  124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAEEL 201
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767999315 237 SILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKR 277
Cdd:COG4717  202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
 
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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