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Conserved domains on  [gi|320542389|ref|NP_730867|]
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transforming acidic coiled-coil protein, isoform I [Drosophila melanogaster]

Protein Classification

transforming acidic coiled-coil-containing protein( domain architecture ID 12059788)

transforming acidic coiled-coil (TACC)-containing protein similar to human TACC1 that is involved in transcription regulation induced by nuclear receptors, including in T3 thyroid hormone and all-trans retinoic acid pathways

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
1008-1218 1.26e-59

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


:

Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 203.37  E-value: 1.26e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1008 HNYNDMDELEKKIKNEVTRsediekklKEGELREeaLIKRITEKDKTNAKLNGVIEAYEKAIAELISEKEQQAQLHERQL 1087
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEE--------KELEINE--LKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEI 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1088 QEVQADRDANYHHLTSLETTFSDLHVKYEKSKEMTSQLKSNEESLLAERKQMMDNLRLQEQRYDKMKNHAMQQLEIANKK 1167
Cdd:pfam05010   71 QKVLEEKDQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEE 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 320542389  1168 LDTYSREHADETKKLKALLKKEEISRVSMTEQLQQKSRENADLLKICEELI 1218
Cdd:pfam05010  151 IAQVRSKAKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
1008-1218 1.26e-59

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 203.37  E-value: 1.26e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1008 HNYNDMDELEKKIKNEVTRsediekklKEGELREeaLIKRITEKDKTNAKLNGVIEAYEKAIAELISEKEQQAQLHERQL 1087
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEE--------KELEINE--LKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEI 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1088 QEVQADRDANYHHLTSLETTFSDLHVKYEKSKEMTSQLKSNEESLLAERKQMMDNLRLQEQRYDKMKNHAMQQLEIANKK 1167
Cdd:pfam05010   71 QKVLEEKDQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEE 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 320542389  1168 LDTYSREHADETKKLKALLKKEEISRVSMTEQLQQKSRENADLLKICEELI 1218
Cdd:pfam05010  151 IAQVRSKAKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
1011-1224 3.21e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 48.50  E-value: 3.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1011 NDMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAELISEKEQQAQLHERQLQEV 1090
Cdd:TIGR00606  867 NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDI 946
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1091 QADRDANYHHLTSLETTFSDLHVKYEKSKE-----MTSQLKSNEEsllaERKQMMDNLRLQEQRYDKMKnhamQQLEIAN 1165
Cdd:TIGR00606  947 KEKVKNIHGYMKDIENKIQDGKDDYLKQKEtelntVNAQLEECEK----HQEKINEDMRLMRQDIDTQK----IQERWLQ 1018
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320542389  1166 KKLDTYSREHADETKKLKALLKKEEISRVSMTEQLQ--QKSRENADLLKICEELIYGKGQG 1224
Cdd:TIGR00606 1019 DNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQehQKLEENIDLIKRNHVLALGRQKG 1079
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1011-1218 6.91e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.68  E-value: 6.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1011 NDMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAELISEKEQQAQLHERQLQEV 1090
Cdd:COG4942    34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1091 QADRDANYHHLTSLETTFSDLHVKYEKSKEMTSQLKSNEESLLAERKQMMDNLRLQEQRYDKMKNhAMQQLEIANKKLDT 1170
Cdd:COG4942   114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA-LLAELEEERAALEA 192
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 320542389 1171 YSREHADETKKLKALLKKEEisrvsmtEQLQQKSRENADLLKICEELI 1218
Cdd:COG4942   193 LKAERQKLLARLEKELAELA-------AELAELQQEAEELEALIARLE 233
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1001-1169 1.54e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1001 TNTEDKTHNYNDMDELEKKIKNE-------VTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAELI 1073
Cdd:PRK03918  155 LGLDDYENAYKNLGEVIKEIKRRierlekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1074 SEKEQQAQLhERQLQEVQADRDANYHHLTSLETTFSDLHVKYEKSKEMTSQLKSNEESLLAERK--QMMDNLRLQEQRYD 1151
Cdd:PRK03918  235 ELKEEIEEL-EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKlsEFYEEYLDELREIE 313
                         170
                  ....*....|....*...
gi 320542389 1152 KMKNHAMQQLEIANKKLD 1169
Cdd:PRK03918  314 KRLSRLEEEINGIEERIK 331
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
1008-1218 1.26e-59

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 203.37  E-value: 1.26e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1008 HNYNDMDELEKKIKNEVTRsediekklKEGELREeaLIKRITEKDKTNAKLNGVIEAYEKAIAELISEKEQQAQLHERQL 1087
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEE--------KELEINE--LKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEI 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1088 QEVQADRDANYHHLTSLETTFSDLHVKYEKSKEMTSQLKSNEESLLAERKQMMDNLRLQEQRYDKMKNHAMQQLEIANKK 1167
Cdd:pfam05010   71 QKVLEEKDQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEE 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 320542389  1168 LDTYSREHADETKKLKALLKKEEISRVSMTEQLQQKSRENADLLKICEELI 1218
Cdd:pfam05010  151 IAQVRSKAKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
1011-1224 3.21e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 48.50  E-value: 3.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1011 NDMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAELISEKEQQAQLHERQLQEV 1090
Cdd:TIGR00606  867 NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDI 946
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1091 QADRDANYHHLTSLETTFSDLHVKYEKSKE-----MTSQLKSNEEsllaERKQMMDNLRLQEQRYDKMKnhamQQLEIAN 1165
Cdd:TIGR00606  947 KEKVKNIHGYMKDIENKIQDGKDDYLKQKEtelntVNAQLEECEK----HQEKINEDMRLMRQDIDTQK----IQERWLQ 1018
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320542389  1166 KKLDTYSREHADETKKLKALLKKEEISRVSMTEQLQ--QKSRENADLLKICEELIYGKGQG 1224
Cdd:TIGR00606 1019 DNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQehQKLEENIDLIKRNHVLALGRQKG 1079
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1011-1144 3.45e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 3.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1011 NDMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAELISEKE------QQAQLHE 1084
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEeleeelEELEAAL 877
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320542389  1085 RQLQE----VQADRDANYHHLTSLETTFSDLHVKYEKSKEMTSQLKSNEESLLAERKQMMDNLR 1144
Cdd:TIGR02169  878 RDLESrlgdLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1011-1218 6.91e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.68  E-value: 6.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1011 NDMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAELISEKEQQAQLHERQLQEV 1090
Cdd:COG4942    34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1091 QADRDANYHHLTSLETTFSDLHVKYEKSKEMTSQLKSNEESLLAERKQMMDNLRLQEQRYDKMKNhAMQQLEIANKKLDT 1170
Cdd:COG4942   114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA-LLAELEEERAALEA 192
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 320542389 1171 YSREHADETKKLKALLKKEEisrvsmtEQLQQKSRENADLLKICEELI 1218
Cdd:COG4942   193 LKAERQKLLARLEKELAELA-------AELAELQQEAEELEALIARLE 233
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1006-1178 7.81e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 7.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1006 KTHNYNDMDELEKKIK---NEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYE-----KAIAELISEKE 1077
Cdd:COG4717    66 PELNLKELKELEEELKeaeEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyqelEALEAELAELP 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1078 QQAQLHERQLQEVQADRDAnyhhLTSLETTFSDLHVKYEKSKEMTSQLKSNEESLLAERKQMmdnLRLQEQRYDKMKNHA 1157
Cdd:COG4717   146 ERLEELEERLEELRELEEE----LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE---LQQRLAELEEELEEA 218
                         170       180
                  ....*....|....*....|.
gi 320542389 1158 MQQLEIANKKLDTYSREHADE 1178
Cdd:COG4717   219 QEELEELEEELEQLENELEAA 239
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1014-1212 4.39e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1014 DELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAEL---ISEKEQQAQLHERQLQEV 1090
Cdd:COG1196   263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELeeeLAELEEELEELEEELEEL 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1091 QADRDANYHHLTSLETTFSDLHvkyEKSKEMTSQLKSNEESLLAERKQMMDNLRLQEQRYDKMKNHAMQQLEIANK--KL 1168
Cdd:COG1196   343 EEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERleRL 419
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 320542389 1169 DTYSREHADETKKLKALLKKEEISRVSMTEQLQQKSRENADLLK 1212
Cdd:COG1196   420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1031-1217 6.32e-04

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: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1031 EKKLKEGEL---REEALIKRITEKDKTNAKLNGVIEAYEKAIAELISEKEQQAQLHERQLQEVQADRDANYHHLTSLETT 1107
Cdd:COG1196   221 ELKELEAELlllKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1108 FSDLHVKYEKSKEMTSQLKSNEESLLAERKQmMDNLRLQEQRYDKMKNHAMQQLEIANKKLdtysREHADETKKLKALLK 1187
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEE-LEELEEELEELEEELEEAEEELEEAEAEL----AEAEEALLEAEAELA 375
                         170       180       190
                  ....*....|....*....|....*....|
gi 320542389 1188 KEEISRVSMTEQLQQKSRENADLLKICEEL 1217
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEEL 405
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1013-1217 6.95e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 6.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1013 MDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIeayeKAIAELISEKEQQAQLH-------ER 1085
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL----YALANEISRLEQQKQILrerlanlER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1086 QLQEVQADRDANYHHLTSLETTFSDLHVKYE---KSKEMTSQLKSNEESLLAERKQMMDNLRLQEQRYDKMKNHAMQQLE 1162
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEelkEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1163 IANKKLDTYSR-----EHADETKKLKALLKKEEISRVSMTEQLQQKSRENADLLKICEEL 1217
Cdd:TIGR02168  397 SLNNEIERLEArlerlEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1011-1156 1.17e-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: 41.83  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1011 NDMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRItekDKTNAKLNGV-----IEAYEKAIAEL---ISEKEQQAQL 1082
Cdd:COG1579    38 DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI---KKYEEQLGNVrnnkeYEALQKEIESLkrrISDLEDEILE 114
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320542389 1083 HERQLQEVQADRDANYHHLTSLETTFSDLHVKYEKSKEmtsQLKSNEESLLAERKQMMDNL--RLQEqRYDKMKNH 1156
Cdd:COG1579   115 LMERIEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEAEREELAAKIppELLA-LYERIRKR 186
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1011-1175 1.42e-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: 43.13  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1011 NDMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRIteKDKTNAKLNGV---IEAYEKAIAEL---ISEKEQQAQLHE 1084
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI--KDLGEEEQLRVkekIGELEAEIASLersIAEKERELEDAE 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1085 RQLQEVQADRDANYHHLTSLETTFSDLHVKYEKSKEMtsqlksneeslLAERKQMMDNLRLQEQRYDKMKNHAMQQLEIA 1164
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE-----------YAELKEELEDLRAELEEVDKEFAETRDELKDY 390
                          170
                   ....*....|.
gi 320542389  1165 NKKLDTYSREH 1175
Cdd:TIGR02169  391 REKLEKLKREI 401
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1001-1169 1.54e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1001 TNTEDKTHNYNDMDELEKKIKNE-------VTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAELI 1073
Cdd:PRK03918  155 LGLDDYENAYKNLGEVIKEIKRRierlekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1074 SEKEQQAQLhERQLQEVQADRDANYHHLTSLETTFSDLHVKYEKSKEMTSQLKSNEESLLAERK--QMMDNLRLQEQRYD 1151
Cdd:PRK03918  235 ELKEEIEEL-EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKlsEFYEEYLDELREIE 313
                         170
                  ....*....|....*...
gi 320542389 1152 KMKNHAMQQLEIANKKLD 1169
Cdd:PRK03918  314 KRLSRLEEEINGIEERIK 331
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
998-1170 1.79e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.65  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389   998 NSNTNTEDKTHNYNDMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEK----DKTNAKLNGVIEAYEKAIAELI 1073
Cdd:pfam02463  308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELeklqEKLEQLEEELLAKKKLESERLS 387
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1074 SEKEQQAQLHERQLQEVQADRDANYH-----HLTSLETTFSDLHVKYEKSKEMTSQLKSNEESL--------LAERKQMM 1140
Cdd:pfam02463  388 SAAKLKEEELELKSEEEKEAQLLLELarqleDLLKEEKKEELEILEEEEESIELKQGKLTEEKEelekqelkLLKDELEL 467
                          170       180       190
                   ....*....|....*....|....*....|
gi 320542389  1141 DNLRLQEQRYDKMKNHAMQQLEIANKKLDT 1170
Cdd:pfam02463  468 KKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1028-1210 2.79e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1028 EDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAEL---ISEKEQQAQLHERQLQEVQADRDANYHHLTSL 1104
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALarrIRALEQELAALEAELAELEKEIAELRAELEAQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1105 ETTFSDLHVKYEKSKEMTSQ--LKSNEESLLAERKQMMDNlRLQEQRYDKMKNHAMQQLEIANKKldtysREHADETKKL 1182
Cdd:COG4942   103 KEELAELLRALYRLGRQPPLalLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALR-----AELEAERAEL 176
                         170       180
                  ....*....|....*....|....*...
gi 320542389 1183 KALLKKEEISRVSMTEQLQQKSRENADL 1210
Cdd:COG4942   177 EALLAELEEERAALEALKAERQKLLARL 204
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1004-1191 2.83e-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: 41.98  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1004 EDKTHNYNDMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAELISEK-EQQAQL 1082
Cdd:TIGR02169  695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIeELEEDL 774
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389  1083 HERQLQEVQADRDANYHHLTSLEttfsdlhvkyEKSKEMTSQLKSNEESLLAERKQMMDNLRLQEQRYDKMKNHAMQQLE 1162
Cdd:TIGR02169  775 HKLEEALNDLEARLSHSRIPEIQ----------AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844
                          170       180
                   ....*....|....*....|....*....
gi 320542389  1163 IANKKLDTYSREHADETKKLKALLKKEEI 1191
Cdd:TIGR02169  845 LKEQIKSIEKEIENLNGKKEELEEELEEL 873
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1012-1096 3.52e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1012 DMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAELISEKEQQAQLHERQLQEVQ 1091
Cdd:COG4942   158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237

                  ....*
gi 320542389 1092 ADRDA 1096
Cdd:COG4942   238 AAAER 242
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
1092-1173 3.85e-03

Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and chromosome partitioning / Signal transduction mechanisms];


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 41.80  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1092 ADRDANYHHLTS-LETTFSDLHVKYEkskEMTSQLKSNEESLLAERkQMMDNLRLQEQRYDKMKNHAMQQLEIANKKLDT 1170
Cdd:COG5261   861 VSRENRYQPLLNeIAKDIINLDALYE---RRRAELDILQDSLRNIC-EHNEYLDSQLQIYGSYLNNARSQLQPKKSKLKG 936

                  ...
gi 320542389 1171 YSR 1173
Cdd:COG5261   937 FSR 939
PRK12704 PRK12704
phosphodiesterase; Provisional
1012-1154 9.61e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 9.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542389 1012 DMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRiTEKDKTNAKLNGVIEAYEKAIA---ELISEKEQQAQLHERQLQ 1088
Cdd:PRK12704   35 EAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLR-NEFEKELRERRNELQKLEKRLLqkeENLDRKLELLEKREEELE 113
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320542389 1089 EVQADRDANYHHLTSLETTFSDLHVKYEKSKEMTSQLkSNEESllaeRKQMMDNLRlQEQRYDKMK 1154
Cdd:PRK12704  114 KKEKELEQKQQELEKKEEELEELIEEQLQELERISGL-TAEEA----KEILLEKVE-EEARHEAAV 173
 
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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