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Conserved domains on  [gi|18405242|ref|NP_564678|]
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DNA double-strand break repair protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 43-233 2.68e-09

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


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 57.77  E-value: 2.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242     43 EDLQIQEGEIRRQDAEIRRLLSDNHGLADDRMVLERELVAAKEELHRMNLMISDLRAEQDLQLREFSEKRHKLEGDVRAM 122
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242    123 ESYKKEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQSDNKQIpgmRAEVKDLQKELMHARDAIEYEKKEKFELMEQR 202
Cdd:TIGR02169  402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK---ALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478

                          170       180       190
                   ....*....|....*....|....*....|.
gi 18405242    203 QTMEKNMVSMAREVEKLRAELATVDSRPWGF 233
Cdd:TIGR02169  479 DRVEKELSKLQRELAEAEAQARASEERVRGG 509
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 43-233 2.68e-09

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: 57.77  E-value: 2.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242     43 EDLQIQEGEIRRQDAEIRRLLSDNHGLADDRMVLERELVAAKEELHRMNLMISDLRAEQDLQLREFSEKRHKLEGDVRAM 122
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242    123 ESYKKEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQSDNKQIpgmRAEVKDLQKELMHARDAIEYEKKEKFELMEQR 202
Cdd:TIGR02169  402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK---ALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478

                          170       180       190
                   ....*....|....*....|....*....|.
gi 18405242    203 QTMEKNMVSMAREVEKLRAELATVDSRPWGF 233
Cdd:TIGR02169  479 DRVEKELSKLQRELAEAEAQARASEERVRGG 509
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 99-226 2.96e-07

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 50.31  E-value: 2.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242  99 AEQDLQLREFSEKRHKLEGDVRAMES----YKKEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQSDNKQIPGMRaEV 174
Cdd:COG1579  13 QELDSELDRLEHRLKELPAELAELEDelaaLEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EY 91

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 18405242 175 KDLQKELMHARDAIEYEKKEKFELMEQRQTMEKNMVSMAREVEKLRAELATV 226
Cdd:COG1579  92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 45-229 2.01e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.80  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242     45 LQIQEGEI--RRQDAEIRRLLSDNHGLADDRMvlerELVAAKEELHRMnlmISDLRAEQDLQLREFSEKRHKLEGDVRAM 122
Cdd:pfam15921  604 LELQEFKIlkDKKDAKIRELEARVSDLELEKV----KLVNAGSERLRA---VKDIKQERDQLLNEVKTSRNELNSLSEDY 676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242    123 E----SYKKEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQSDN-----------KQIPGMRAEVKDLQKELMHARDA 187
Cdd:pfam15921  677 EvlkrNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDghamkvamgmqKQITAKRGQIDALQSKIQFLEEA 756

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 18405242    188 IEYEKKEKFELMEQRQTMEKNMVSMAREVEKLRAELATVDSR 229
Cdd:pfam15921  757 MTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQ 798
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
76-229 1.74e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242   76 LERELVAAKEELHRMNLMISDLRAEqdlqLREFSEKRHKLEGDVRAMESYKKEASQLRGEVQKLDEIKRELSGNVQLLRK 155
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSE----LPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE 266

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18405242  156 DLAKLQSDNKQIPGMRAEVKDLQKElmhardAIEYEKKEKF--ELMEQRQTMEKNMVSMAREVEKLRAELATVDSR 229
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEK------AEEYIKLSEFyeEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 104-223 7.90e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 37.30  E-value: 7.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242    104 QLREFSEKRHKLEGDVRAmesyKKEAsqLRGEVQKLDEIKRELSGNVQ-LLRKDLAKLQSDNKQIPGMRAEVKDLQKELM 182
Cdd:smart00787 162 LLMKELELLNSIKPKLRD----RKDA--LEEELRQLKQLEDELEDCDPtELDRAKEKLKKLLQEIMIKVKKLEELEEELQ 235

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 18405242    183 HARDAIEYEKKEKFELMEQ----RQTMEKNMVSMAREVEKLRAEL 223
Cdd:smart00787 236 ELESKIEDLTNKKSELNTEiaeaEKKLEQCRGFTFKEIEKLKEQL 280
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 43-233 2.68e-09

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: 57.77  E-value: 2.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242     43 EDLQIQEGEIRRQDAEIRRLLSDNHGLADDRMVLERELVAAKEELHRMNLMISDLRAEQDLQLREFSEKRHKLEGDVRAM 122
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242    123 ESYKKEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQSDNKQIpgmRAEVKDLQKELMHARDAIEYEKKEKFELMEQR 202
Cdd:TIGR02169  402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK---ALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478

                          170       180       190
                   ....*....|....*....|....*....|.
gi 18405242    203 QTMEKNMVSMAREVEKLRAELATVDSRPWGF 233
Cdd:TIGR02169  479 DRVEKELSKLQRELAEAEAQARASEERVRGG 509
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 49-223 7.20e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 7.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242     49 EGEIRRQDAEIRRLLSDNHGLADDRMVLERELVAAKEELHRMNLMISDLRAEQDLQLREFSEKRHKLEGDVRAMESYKKE 128
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242    129 ASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQSDNKQ----IPGMRAEVKDLQKELMHARdaIEYEKKEKFELMEQRQT 204
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERlqqeIEELLKKLEEAELKELQAE--LEELEEELEELQEELER 458

                          170
                   ....*....|....*....
gi 18405242    205 MEKNMVSMAREVEKLRAEL 223
Cdd:TIGR02168  459 LEEALEELREELEEAEQAL 477
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 99-226 2.96e-07

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 50.31  E-value: 2.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242  99 AEQDLQLREFSEKRHKLEGDVRAMES----YKKEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQSDNKQIPGMRaEV 174
Cdd:COG1579  13 QELDSELDRLEHRLKELPAELAELEDelaaLEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EY 91

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 18405242 175 KDLQKELMHARDAIEYEKKEKFELMEQRQTMEKNMVSMAREVEKLRAELATV 226
Cdd:COG1579  92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 43-223 5.37e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 5.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242     43 EDLQIQEGEIRRQDAEIRRLLSDNHGLADDRMVLERELVAAKEELHRMNLMISDLRAEQDLQLREFSEKRHKLEGDVRAM 122
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242    123 ESYKKEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQsdnKQIPGMRAEVKDLQKELMHARDAIEYEKKEKFELMEQR 202
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE---ELIEELESELEALLNERASLEEALALLRSELEELSEEL 903

                          170       180
                   ....*....|....*....|.
gi 18405242    203 QTMEKnmvsmarEVEKLRAEL 223
Cdd:TIGR02168  904 RELES-------KRSELRREL 917
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 43-229 5.67e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.15  E-value: 5.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242  43 EDLQIQEGEIRRQDAEIRRLLSDNHGLADDRMVLERELVAAKEELHRMNLMISDLRAEQDLQLREFSEKRHKLEGDVRAM 122
Cdd:COG4942  34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242 123 ESYK-----------KEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQSDNKQIPGMRAEVKDLQKELMHARDAIEYE 191
Cdd:COG4942 114 YRLGrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 18405242 192 KKEKFELM----EQRQTMEKNMVSMAREVEKLRAELATVDSR 229
Cdd:COG4942 194 KAERQKLLarleKELAELAAELAELQQEAEELEALIARLEAE 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 55-224 1.11e-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: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242     55 QDAEIRRLLSDNHGLADDRMVLERELVAAKEELHRMNLMISDLRAEQDLQLREFSEKRHKLEGDVRAMESYKKEASQLRG 134
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242    135 EVQKLDEIKRE----LSGNVQLLRKDLAKLQSDNKQIPGMRAEVKDLQKELMHARDAIEYEKKEKFELMEQRQTMEKNMV 210
Cdd:TIGR02168  755 ELTELEAEIEEleerLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834

                          170
                   ....*....|....
gi 18405242    211 SMAREVEKLRAELA 224
Cdd:TIGR02168  835 ATERRLEDLEEQIE 848
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
18-168 1.49e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 49.09  E-value: 1.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242  18 HRDLPPERPflrgppLLQPPPPSLLEDLQIQEGEIRRQDAEIRRLLSDNhgladdrMVLERELVAAKEELHRMNLMISDL 97
Cdd:COG2433 387 EKELPEEEP------EAEREKEHEERELTEEEEEIRRLEEQVERLEAEV-------EELEAELEEKDERIERLERELSEA 453

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18405242  98 RAEQDLQLREfsekrhklegdVRAMESYKKEASQLRGEVQKLDEIKRELSGNVQLLRKdLAKLQSDNKQIP 168
Cdd:COG2433 454 RSEERREIRK-----------DREISRLDREIERLERELEEERERIEELKRKLERLKE-LWKLEHSGELVP 512
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 43-224 2.21e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 2.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242  43 EDLQIQEGEIRRQDAEIRRLLSDNHGLADDRMVLERELVAAKEELHRMNLMISDLRAEQDLQLREFSEKRHKLEGDVRAM 122
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242 123 ESYKKEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQSDNKQipgMRAEVKDLQKELMHARDAIEYEKKEKFELMEQR 202
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER---LEEELEELEEALAELEEEEEEEEEALEEAAEEE 451

                       170       180
                ....*....|....*....|..
gi 18405242 203 QTMEKNMVSMAREVEKLRAELA 224
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAA 473
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
43-225 2.10e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242   43 EDLQIQEGEIRRQDAEIRRLLSDNHGLADDRmvLERELVAAKEELHRMNLMISDLRAEQDLQLREFSEKRHKLEG-DVRA 121
Cdd:COG4913  262 ERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDR 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242  122 MESYKKEASQLRgevQKLDEIKRELSGNVQLLR----------KDLAKLQsdnKQIPGMRAEVKDLQKELMHARDAIEYE 191
Cdd:COG4913  340 LEQLEREIERLE---RELEERERRRARLEALLAalglplpasaEEFAALR---AEAAALLEALEEELEALEEALAEAEAA 413

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 18405242  192 ----KKEKFELMEQRQTMEKNMVSMAREVEKLRAELAT 225
Cdd:COG4913  414 lrdlRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 44-229 8.97e-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: 43.89  E-value: 8.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242     44 DLQIQEGEIRRQDAEIRRLLSDNHGLADDRMVLERELVAAKEELHRMNLMISDLRAEQDLQLREFSEKRHKLEGDVRAME 123
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242    124 SYKKEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQsdnKQIPGMRAEVKDLQKELMHARDAIEYEKKEKFELMEQRQ 203
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELE---EKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382

                          170       180
                   ....*....|....*....|....*.
gi 18405242    204 TMEKNMVSMAREVEKLRAELATVDSR 229
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLEAR 408
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 43-225 1.75e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242  43 EDLQIQEGEIRRQDAEIRRLLSDNHGLADDRMVLERELVAAKEELHRMNLMISDLRAEQDLQLREFSEKRHKLEgdvRAM 122
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE---EAE 357

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242 123 ESYKKEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQSDNKQIPGMRAEVKDLQKELMHARDAIEYEKKEKFELMEQR 202
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437

                       170       180
                ....*....|....*....|...
gi 18405242 203 QTMEKNMVSMAREVEKLRAELAT 225
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEA 460
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 45-229 2.01e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.80  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242     45 LQIQEGEI--RRQDAEIRRLLSDNHGLADDRMvlerELVAAKEELHRMnlmISDLRAEQDLQLREFSEKRHKLEGDVRAM 122
Cdd:pfam15921  604 LELQEFKIlkDKKDAKIRELEARVSDLELEKV----KLVNAGSERLRA---VKDIKQERDQLLNEVKTSRNELNSLSEDY 676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242    123 E----SYKKEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQSDN-----------KQIPGMRAEVKDLQKELMHARDA 187
Cdd:pfam15921  677 EvlkrNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDghamkvamgmqKQITAKRGQIDALQSKIQFLEEA 756

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 18405242    188 IEYEKKEKFELMEQRQTMEKNMVSMAREVEKLRAELATVDSR 229
Cdd:pfam15921  757 MTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQ 798
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-229 2.38e-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: 42.35  E-value: 2.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242     94 ISDLRAEQDLQLREFSEKRHKLegdvramESYKKEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQsdnKQIPGMRAE 173
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKAL-------AELRKELEELEEELEQLRKELEELSRQISALRKDLARLE---AEVEQLEER 748

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 18405242    174 VKDLQKELMHARDAIEYEKKEKFELMEQRQTMEKNMVSMAREVEKLRAELATVDSR 229
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 77-229 2.61e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242  77 ERELVAAKEELHRmnlmISDLRAEQDLQL-------------REFSEKRHKLEGDVRA--MESYKKEASQLRGEVQKLDE 141
Cdd:COG1196 178 ERKLEATEENLER----LEDILGELERQLeplerqaekaeryRELKEELKELEAELLLlkLRELEAELEELEAELEELEA 253

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242 142 IKRELSGNVQLLRKDLAKLQSDNKQIpgmRAEVKDLQKELMHARDAIEYEKKEKFELMEQRQTMEKNMVSMAREVEKLRA 221
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEEL---ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330


                ....*...
gi 18405242 222 ELATVDSR 229
Cdd:COG1196 331 ELEELEEE 338
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
76-229 1.74e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242   76 LERELVAAKEELHRMNLMISDLRAEqdlqLREFSEKRHKLEGDVRAMESYKKEASQLRGEVQKLDEIKRELSGNVQLLRK 155
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSE----LPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE 266

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18405242  156 DLAKLQSDNKQIPGMRAEVKDLQKElmhardAIEYEKKEKF--ELMEQRQTMEKNMVSMAREVEKLRAELATVDSR 229
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEK------AEEYIKLSEFyeEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 76-224 2.13e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 2.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242  76 LERELVAAKEELHRMNLMISDLRAEQDLQLREFSEKRHKLEGDVRAMESYKKEASQLRGEVQKLDEIKRELSGNVQLLRK 155
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18405242 156 DLAKLQSDNKQIpgmRAEVKDLQKELMHARDAIEYEKKEKFELMEQRQTMEKNMVSMAREVEKLRAELA 224
Cdd:COG1196 317 RLEELEEELAEL---EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 56-209 2.28e-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: 2.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242  56 DAEIRRLLSDNHGLADDRMVLERELVAAKEELHRMNLMISDLRAEQ---DLQLREFSEKRHKLEG------DVRAMESYK 126
Cdd:COG1579  16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrlELEIEEVEARIKKYEEqlgnvrNNKEYEALQ 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242 127 KEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQSDNKQIpgmRAEVKDLQKELmhaRDAIEYEKKEKFELMEQRQTME 206
Cdd:COG1579  96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAEL---EAELEEKKAEL---DEELAELEAELEELEAEREELA 169


                ...
gi 18405242 207 KNM 209
Cdd:COG1579 170 AKI 172
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
49-228 3.11e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 3.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242   49 EGEIRRQDAEIRRLlsdnHGLADDRMVLERELVAAKEELhrmnlmisdlrAEQDLQLREFS-EKRHKLEGDVRAMESYKK 127
Cdd:PRK03918 538 KGEIKSLKKELEKL----EELKKKLAELEKKLDELEEEL-----------AELLKELEELGfESVEELEERLKELEPFYN 602

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242  128 EASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQSDNKQIPGMRAEVKDLQK---ELMHARDAIEYEKKEK--FELMEQR 202
Cdd:PRK03918 603 EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkysEEEYEELREEYLELSRelAGLRAEL 682

                        170       180
                 ....*....|....*....|....*.
gi 18405242  203 QTMEKNMVSMAREVEKLRAELATVDS 228
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEEREK 708
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
69-218 5.60e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 37.58  E-value: 5.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242  69 LADDRMVLERELVAAKEELHRMNLMISDLRAEQDlqlrefsEKRHKLEGDVRAMESYKKEASQLRGEVQKLDEIKRELSG 148
Cdd:COG1340  13 LEEKIEELREEIEELKEKRDELNEELKELAEKRD-------ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18405242 149 NVQLLRKDLAKLQSDNKQIPGMRAEVKDLQKELMHARDAIEYE----KKEKfELMEQRQTMEKNMVSMAREVEK 218
Cdd:COG1340  86 KLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEvlspEEEK-ELVEKIKELEKELEKAKKALEK 158
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
76-201 6.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242   76 LERELVAAKEELHRMNLMISDLRAEQDLQLREFSEKRHklegdvramESYKKEASQLRGEVQKLDEIKRELSGNVQLLRK 155
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY---------EELREEYLELSRELAGLRAELEELEKRREEIKK 694

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 18405242  156 DLAKLQSDNKQIPGMRAEVKDLQKELMHARDAIEYEKKEKFELMEQ 201
Cdd:PRK03918 695 TLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 104-223 7.90e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 37.30  E-value: 7.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242    104 QLREFSEKRHKLEGDVRAmesyKKEAsqLRGEVQKLDEIKRELSGNVQ-LLRKDLAKLQSDNKQIPGMRAEVKDLQKELM 182
Cdd:smart00787 162 LLMKELELLNSIKPKLRD----RKDA--LEEELRQLKQLEDELEDCDPtELDRAKEKLKKLLQEIMIKVKKLEELEEELQ 235

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 18405242    183 HARDAIEYEKKEKFELMEQ----RQTMEKNMVSMAREVEKLRAEL 223
Cdd:smart00787 236 ELESKIEDLTNKKSELNTEiaeaEKKLEQCRGFTFKEIEKLKEQL 280
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 43-275 8.28e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.50  E-value: 8.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242  43 EDLQIQEGEIRRQDAEIRRLLSDNHGLADDRMVLERELVAAKEELHRMNLMISDLRAEQDLQLR---------------- 106
Cdd:COG3883  30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARalyrsggsvsyldvll 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242 107 ------EFSEKRHKLEgdvRAMESYKKEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQSDNKQIPGMRAEVKDLQKE 180
Cdd:COG3883 110 gsesfsDFLDRLSALS---KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242 181 LmhaRDAIEYEKKEKFELMEQRQTMEKNMVSMAREVEKLRAELATVDSRPWGFGGSYGMNYNNMDGTFRGSYGENDTYLG 260
Cdd:COG3883 187 L---SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263

                       250
                ....*....|....*
gi 18405242 261 SSERSQYYSHGSGSQ 275
Cdd:COG3883 264 AAGAAAGAAGAGAAA 278
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 43-225 8.74e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 37.69  E-value: 8.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242    43 EDLQIQEGEIRRQDAEIRRLLSDNHGLADDRMVLERELVAAKEELHRMNLMISDLRAEQDLQLREFSEKRHKLEGDVRAM 122
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405242   123 ESYKKEASQLRGEVQKLDEIKRELSGNVQLLRKDLAKLQSDNKQIpgmRAEVKDLQKELMH-----ARDAIEYEKKEKFE 197
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK---ESKISDLEDELNKddfelKKENLEKEIDEKNK 568

                         170       180
                  ....*....|....*....|....*...
gi 18405242   198 LMEQRQTMEKNMVSMAREVEKLRAELAT 225
Cdd:TIGR04523 569 EIEELKQTQKSLKKKQEEKQELIDQKEK 596
 
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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