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Conserved domains on  [gi|13376818|ref|NP_079490|]
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coiled-coil domain-containing protein 68 [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 ...
 94-304 4.20e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 4.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818     94 KIKGKDLQLLEMNKENEVLKiKLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLlQVNKLEKEQKLKQHVEN 173
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELE-EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL-EAQLEELESKLDELAEE 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818    174 LNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKS-SATYGKSCQDLQREISILQEQISHLQFVIHS 252
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQLELQIASLNNEIERLEARLERLEDRRER 418

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 13376818    253 QHQNLRSVIQ-----EMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVALSSE 304
Cdd:TIGR02168  419 LQQEIEELLKkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-304 4.20e-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: 51.60  E-value: 4.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818     94 KIKGKDLQLLEMNKENEVLKiKLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLlQVNKLEKEQKLKQHVEN 173
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELE-EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL-EAQLEELESKLDELAEE 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818    174 LNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKS-SATYGKSCQDLQREISILQEQISHLQFVIHS 252
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQLELQIASLNNEIERLEARLERLEDRRER 418

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 13376818    253 QHQNLRSVIQ-----EMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVALSSE 304
Cdd:TIGR02168  419 LQQEIEELLKkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 88-300 1.48e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  88 LDLLMKKIKGKDLQLLEMNKENEVLKIKLQASREAGAAALRnvAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKL 167
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQA--EEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818 168 KQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQ-LKSSATYGKSCQDLQREISILQEQISHL 246
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEaEEELEELAEELLEALRAAAELAAQLEEL 405

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 13376818 247 QFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVA 300
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 140-296 7.29e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 44.53  E-value: 7.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  140 TQSEEVRKKQEDSKQLLQVNKLEKeqkLKQHVE-NLNQVAEKLEEKHSQITELENLVQRMEKEKRtLLE--RKLSLENKL 216
Cdd:PRK05771  63 RSYLPKLNPLREEKKKVSVKSLEE---LIKDVEeELEKIEKEIKELEEEISELENEIKELEQEIE-RLEpwGNFDLDLSL 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  217 LQLKSSATYGKSCQDLQREISILQEQISHLQFVIH--------------SQHQNLRSVIQEMEGLKNNLKEQ---DKRIE 279
Cdd:PRK05771 139 LLGFKYVSVFVGTVPEDKLEELKLESDVENVEYIStdkgyvyvvvvvlkELSDEVEEELKKLGFERLELEEEgtpSELIR 218

                        170
                 ....*....|....*..
gi 13376818  280 NLREKVNILEAQNKELK 296
Cdd:PRK05771 219 EIKEELEEIEKERESLL 235
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 110-301 6.03e-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: 41.42  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818   110 EVLKIKLQASREAgaaalRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQIT 189
Cdd:pfam07888  30 ELLQNRLEECLQE-----RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818   190 ELENLVQRMEKEKRTLLERKLSLENKLLQLKS-SATYGKSCQDLQREISILQEQI--------------SHLQFVIHSQH 254
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRELEEdIKTLTQRVLERETELERMKERAkkagaqrkeeeaerKQLQAKLQQTE 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 13376818   255 QNLRSVIQEMEGLKNNLKEQDKRIENLREKVNIL-----EAQNKELKTQVAL 301
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqkltTAHRKEAENEALL 236
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-304 4.20e-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: 51.60  E-value: 4.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818     94 KIKGKDLQLLEMNKENEVLKiKLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLlQVNKLEKEQKLKQHVEN 173
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELE-EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL-EAQLEELESKLDELAEE 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818    174 LNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKS-SATYGKSCQDLQREISILQEQISHLQFVIHS 252
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQLELQIASLNNEIERLEARLERLEDRRER 418

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 13376818    253 QHQNLRSVIQ-----EMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVALSSE 304
Cdd:TIGR02168  419 LQQEIEELLKkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 87-298 1.05e-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: 50.44  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818     87 SLDLLMKKIKGKDLQLLEMNKENEVLKIKLQASREAGAAALRNVAQRLFEnyQTQSEEVRKKQEDSKQLLQVNKLEKEQK 166
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE--LTELEAEIEELEERLEEAEEELAEAEAE 783

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818    167 LKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSATY-GKSCQDLQREISILQEQISH 245
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDlEEQIEELSEDIESLAAEIEE 863

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 13376818    246 LQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQ 298
Cdd:TIGR02168  864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 88-300 1.48e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  88 LDLLMKKIKGKDLQLLEMNKENEVLKIKLQASREAGAAALRnvAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKL 167
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQA--EEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818 168 KQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQ-LKSSATYGKSCQDLQREISILQEQISHL 246
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEaEEELEELAEELLEALRAAAELAAQLEEL 405

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 13376818 247 QFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVA 300
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 101-300 1.48e-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: 1.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818    101 QLLEMNKENEvlkiKLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQK--LKQHVENLNQVA 178
Cdd:TIGR02169  675 ELQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerLEELEEDLSSLE 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818    179 EKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSaTYGKSCQDLQREISILQEQISHLQFVIHSQHQNLR 258
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP-EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 13376818    259 SVIQEMEG-------LKNNLKEQDKRIENLREKVNILEAQNKELKTQVA 300
Cdd:TIGR02169  830 YLEKEIQElqeqridLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 88-300 2.18e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  88 LDLLMKKIKGKDLQLLEMNKENEVLKIKLQAsREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLlqvnklekEQKL 167
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEEAQAEEYELLAELARL--------EQDI 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818 168 KQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSAtygkscQDLQREISILQEQISHLQ 247
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL------AEAEEALLEAEAELAEAE 378

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 13376818 248 FVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVA 300
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 161-300 2.85e-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: 48.90  E-value: 2.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818    161 LEKEQKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSA--------TYGKSCQDL 232
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLarleaeveQLEERIAQL 752

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13376818    233 QREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVA 300
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 120-299 4.42e-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: 4.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818    120 REAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLlQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQITELENLVQRME 199
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKEAEEELEEL-TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818    200 KEKRTLLERKLSLENKLLQLK-SSATYGKSCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRI 278
Cdd:TIGR02168  302 QQKQILRERLANLERQLEELEaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381

                          170       180
                   ....*....|....*....|.
gi 13376818    279 ENLREKVNILEAQNKELKTQV 299
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEI 402
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 140-296 7.29e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 44.53  E-value: 7.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  140 TQSEEVRKKQEDSKQLLQVNKLEKeqkLKQHVE-NLNQVAEKLEEKHSQITELENLVQRMEKEKRtLLE--RKLSLENKL 216
Cdd:PRK05771  63 RSYLPKLNPLREEKKKVSVKSLEE---LIKDVEeELEKIEKEIKELEEEISELENEIKELEQEIE-RLEpwGNFDLDLSL 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  217 LQLKSSATYGKSCQDLQREISILQEQISHLQFVIH--------------SQHQNLRSVIQEMEGLKNNLKEQ---DKRIE 279
Cdd:PRK05771 139 LLGFKYVSVFVGTVPEDKLEELKLESDVENVEYIStdkgyvyvvvvvlkELSDEVEEELKKLGFERLELEEEgtpSELIR 218

                        170
                 ....*....|....*..
gi 13376818  280 NLREKVNILEAQNKELK 296
Cdd:PRK05771 219 EIKEELEEIEKERESLL 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 115-300 8.73e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 8.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818 115 KLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQITELENL 194
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818 195 VQRMEKEKRTLLERKLSLENKLLQLKSS-ATYGKSCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKE 273
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEElAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376

                       170       180
                ....*....|....*....|....*..
gi 13376818 274 QDKRIENLREKVNILEAQNKELKTQVA 300
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLE 403
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
178-300 1.08e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  178 AEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSATYGKSCQD---LQREISILQEQISHLQfvihSQH 254
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasAEREIAELEAELERLD----ASS 684

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 13376818  255 QNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVA 300
Cdd:COG4913  685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
116-305 1.88e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 1.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818 116 LQASREAGAAALRNVAQRLfENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKlkQHVENLNQVAEKLEEKHSQITELENLV 195
Cdd:COG3206 166 LELRREEARKALEFLEEQL-PELRKELEEAEAALEEFRQKNGLVDLSEEAK--LLLQQLSELESQLAEARAELAEAEARL 242

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818 196 QRMEKEKRT----------------LLERKLSLENKLLQLksSATYGKSCQDLQReisiLQEQISHLQFVIHSQHQNLRS 259
Cdd:COG3206 243 AALRAQLGSgpdalpellqspviqqLRAQLAELEAELAEL--SARYTPNHPDVIA----LRAQIAALRAQLQQEAQRILA 316

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 13376818 260 VIQ-EMEGLKNNLKEQDKRIENLREKVNIL---EAQNKELKTQVALSSET 305
Cdd:COG3206 317 SLEaELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVAREL 366
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
150-285 1.97e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.92  E-value: 1.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818 150 EDSKQLLQVNKLEKEQKLKQHVE-NLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSAtygKS 228
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEErELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE---RR 459

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13376818 229 CQDLQREISILQEQIShlqfvihsqhqNLRSVIQEMEGLKNNLKEQDKRIENLREKV 285
Cdd:COG2433 460 EIRKDREISRLDREIE-----------RLERELEEERERIEELKRKLERLKELWKLE 505
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
117-287 1.98e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  117 QASREAGAAALRNVAQRLFEnyQTQSEEVRKKQEDSKQLLQVNKLEKEQkLKQHVENLNQVAEKLEEKHSQ-----ITEL 191
Cdd:COG4913  267 ARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELER-LEARLDALREELDELEAQIRGnggdrLEQL 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  192 ENLVQRMEKEKRTLLERKLSLENKLLQLKSSATYGKscQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNL 271
Cdd:COG4913  344 EREIERLERELEERERRRARLEALLAALGLPLPASA--EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421

                        170
                 ....*....|....*..
gi 13376818  272 KEQDKRIENLRE-KVNI 287
Cdd:COG4913  422 RELEAEIASLERrKSNI 438
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 124-300 4.20e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 4.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818 124 AAALRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKLKQhvenLNQVAEKLEEKHSQITELENLVQRMEKEKR 203
Cdd:COG4942  11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEQELAALEAELA 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818 204 TLLERKLSLENKLLQLKssatygkscQDLQREISILQ--EQISHLQFVIHSqhQNLRSVIQEMEGLKNNLKEQDKRIENL 281
Cdd:COG4942  87 ELEKEIAELRAELEAQK---------EELAELLRALYrlGRQPPLALLLSP--EDFLDAVRRLQYLKYLAPARREQAEEL 155

                       170
                ....*....|....*....
gi 13376818 282 REKVNILEAQNKELKTQVA 300
Cdd:COG4942 156 RADLAELAALRAELEAERA 174
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 101-295 5.28e-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: 41.97  E-value: 5.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818    101 QLLEMNKENEVLKIKLQASREAgAAALRNVAQRLFENYQTQSEEVRKKQ------EDSKQLLQVNKLEKEQKLKQHVENL 174
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALREA-LDELRAELTLLNEEAANLRERLESLErriaatERRLEDLEEQIEELSEDIESLAAEI 861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818    175 NQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSATYGK-SCQDLQREISILQEQISHLQFVIHSQ 253
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRrELEELREKLAQLELRLEGLEVRIDNL 941

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 13376818    254 HQNLRSVIQ-EMEGLKNNLKEQDKRIENLREKVNILEAQNKEL 295
Cdd:TIGR02168  942 QERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 110-301 6.03e-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: 41.42  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818   110 EVLKIKLQASREAgaaalRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQIT 189
Cdd:pfam07888  30 ELLQNRLEECLQE-----RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818   190 ELENLVQRMEKEKRTLLERKLSLENKLLQLKS-SATYGKSCQDLQREISILQEQI--------------SHLQFVIHSQH 254
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRELEEdIKTLTQRVLERETELERMKERAkkagaqrkeeeaerKQLQAKLQQTE 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 13376818   255 QNLRSVIQEMEGLKNNLKEQDKRIENLREKVNIL-----EAQNKELKTQVAL 301
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqkltTAHRKEAENEALL 236
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 156-300 6.86e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 6.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818    156 LQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEK-----------EKRTLLERKLSLENKLLQLKSSAT 224
Cdd:TIGR02168  170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELK 249

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13376818    225 -YGKSCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVA 300
Cdd:TIGR02168  250 eAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
134-300 8.67e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 8.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818 134 LFENYQTQSEEVRKKQ--EDSKQLLQVNKLEKE-QKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTL----- 205
Cdd:COG4717  47 LLERLEKEADELFKPQgrKPELNLKELKELEEElKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekllq 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818 206 ----LERKLSLENKLL----QLKSSATYGKSCQDLQREISILQEQISHLQFVIHSQHQNLR-SVIQEMEGLKNNLKEQDK 276
Cdd:COG4717 127 llplYQELEALEAELAelpeRLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQ 206

                       170       180
                ....*....|....*....|....
gi 13376818 277 RIENLREKVNILEAQNKELKTQVA 300
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELE 230
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 172-296 2.00e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.81  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  172 ENLNQVAEKLEEKH----SQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSATygkscQDLQREISILQEQISHLQ 247
Cdd:PRK00409 516 EKLNELIASLEELEreleQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAE-----KEAQQAIKEAKKEADEII 590

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 13376818  248 FVIHSQHQNLRSVIQEMEgLKNNLKEQDKRIENLREKVNILEAQNKELK 296
Cdd:PRK00409 591 KELRQLQKGGYASVKAHE-LIEARKRLNKANEKKEKKKKKQKEKQEELK 638
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 149-300 2.49e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 2.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818 149 QEDSKQLLQVNKLEKE--QKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSATYg 226
Cdd:COG1579  13 QELDSELDRLEHRLKElpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEY- 91

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13376818 227 kscQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKvniLEAQNKELKTQVA 300
Cdd:COG1579  92 ---EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELE 159
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
113-293 3.58e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 3.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818 113 KIKLQASREAGAAALRNVAQRL---FENYQTQSEEVRKKQEDSKQLLQVNKLEKE-QKLKQHVENLNQVAEKLEEKHSQI 188
Cdd:COG4717  79 ELKEAEEKEEEYAELQEELEELeeeLEELEAELEELREELEKLEKLLQLLPLYQElEALEAELAELPERLEELEERLEEL 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818 189 TELENLVQRMEKEKRTLLERklslENKLLQLKSSATYgKSCQDLQREISILQEQISHLQfvihsqhqnlrsviQEMEGLK 268
Cdd:COG4717 159 RELEEELEELEAELAELQEE----LEELLEQLSLATE-EELQDLAEELEELQQRLAELE--------------EELEEAQ 219

                       170       180
                ....*....|....*....|....*
gi 13376818 269 NNLKEQDKRIENLREKVNILEAQNK 293
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEER 244
PRK12704 PRK12704
phosphodiesterase; Provisional
 90-218 4.37e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 4.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818   90 LLMKKIKGKDLQllemNKENEVLKIKLQASREAGAA---ALRNvAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQK 166
Cdd:PRK12704  23 FVRKKIAEAKIK----EAEEEAKRILEEAKKEAEAIkkeALLE-AKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEN 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 13376818  167 LKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEkrtlLERKLSLENKLLQ 218
Cdd:PRK12704  98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEE----LEELIEEQLQELE 145
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
142-296 5.34e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 5.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  142 SEEVRKKQedSKQLLQVNKLEK-EQKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLK 220
Cdd:PRK03918 143 SDESREKV--VRQILGLDDYENaYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR 220

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13376818  221 SSAtygkscqdlqREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELK 296
Cdd:PRK03918 221 EEL----------EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
147-318 5.58e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 5.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  147 KKQEDSKQLLQVNKLEKE-QKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLEN-------KLLQ 218
Cdd:PRK03918 198 KEKELEEVLREINEISSElPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEErieelkkEIEE 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  219 LKSSATYGKSCQDLQREISILQE----------QISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNIL 288
Cdd:PRK03918 278 LEEKVKELKELKEKAEEYIKLSEfyeeyldelrEIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL 357

                        170       180       190
                 ....*....|....*....|....*....|
gi 13376818  289 EAQNKELKTQVALSSETPRTKVSKAVSTSE 318
Cdd:PRK03918 358 EERHELYEEAKAKKEELERLKKRLTGLTPE 387
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 101-299 6.11e-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: 6.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818    101 QLLEMNKENEVLKIKLQASREAGAAALRNVAQRLfENYQTQSEEVRKKQEDSKQLLQvnklEKEQKLKQHVENLNQVAEK 180
Cdd:TIGR02169  319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRR-DKLTEEYAELKEELEDLRAELE----EVDKEFAETRDELKDYREK 393

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818    181 LEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSATygkscqDLQREISILQEQISHLQFVIHSQHQNLRSV 260
Cdd:TIGR02169  394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN------ELEEEKEDKALEIKKQEWKLEQLAADLSKY 467

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 13376818    261 IQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQV 299
Cdd:TIGR02169  468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
113-285 6.33e-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: 6.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  113 KIKLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKE-QKLKQHVENLNQVAEKLEEKHS----- 186
Cdd:COG4913  611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDASSDdlaal 690

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  187 --QITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSAtygKSCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEM 264
Cdd:COG4913  691 eeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL---DELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767

                        170       180
                 ....*....|....*....|..
gi 13376818  265 -EGLKNNLKEQDKRIENLREKV 285
Cdd:COG4913  768 rENLEERIDALRARLNRAEEEL 789
COG5022 COG5022
Myosin heavy chain [General function prediction only];
111-335 7.53e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 38.14  E-value: 7.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  111 VLKIKLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQITE 190
Cdd:COG5022  831 KLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIE 910

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  191 LENLVQRMEKEKRTLLERKLSLENKLLQlKSSATYGKSCQ-DLQREISILQEQISHLQFV------IHSQHQNLRS---- 259
Cdd:COG5022  911 LKKSLSSDLIENLEFKTELIARLKKLLN-NIDLEEGPSIEyVKLPELNKLHEVESKLKETseeyedLLKKSTILVRegnk 989

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818  260 VIQEMEGLKNNLKE---QDKRIENLREKVNILEAQNKELKTQVALSSETP-----RTKVSKAVSTSELKTEGVSPYLMLI 331
Cdd:COG5022  990 ANSELKNFKKELAElskQYGALQESTKQLKELPVEVAELQSASKIISSEStelsiLKPLQKLKGLLLLENNQLQARYKAL 1069


                 ....
gi 13376818  332 RLRK 335
Cdd:COG5022 1070 KLRR 1073
mukB PRK04863
chromosome partition protein MukB;
118-303 7.99e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.01  E-value: 7.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818   118 ASREAGAAALRNVAQRLFENYQTQSEEVRKKQ---EDSKQLLQVN-----KLEKEQKLKQHVENLNQVAEKLEEKHSQIT 189
Cdd:PRK04863  782 AAREKRIEQLRAEREELAERYATLSFDVQKLQrlhQAFSRFIGSHlavafEADPEAELRQLNRRRVELERALADHESQEQ 861

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818   190 ELENLVQRMeKEKRTLLERKLSLENKLLQlkssATYGKSCQDLQREISILQEQISHLQfvihsQHQNLrsvIQEMEGLKN 269
Cdd:PRK04863  862 QQRSQLEQA-KEGLSALNRLLPRLNLLAD----ETLADRVEEIREQLDEAEEAKRFVQ-----QHGNA---LAQLEPIVS 928

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 13376818   270 NLKEQDKRIENLREKVNILEAQNKELKTQV-ALSS 303
Cdd:PRK04863  929 VLQSDPEQFEQLKQDYQQAQQTQRDAKQQAfALTE 963
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 131-218 9.75e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 37.27  E-value: 9.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376818   131 AQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKLKQHVENLNQVAEKLE-EKHSQITELENLVQRMEKEKRTLLERK 209
Cdd:pfam02841 202 KEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEaEREQLLAEQERMLEHKLQEQEELLKEG 281


                  ....*....
gi 13376818   210 LSLENKLLQ 218
Cdd:pfam02841 282 FKTEAESLQ 290
 
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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