NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1847688279|ref|NP_001371079|]
View 

paralemmin-2 isoform 4 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MYO6_MIU_linker super family cl46503
MIU-linker domain found in unconventional myosin-VI; Myosins are actin-based motor molecules ...
 15-117 2.02e-41

MIU-linker domain found in unconventional myosin-VI; Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins function in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. It appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by the MYO6 gene, the human homologue of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant nonsyndromic hearing loss. This model corresponds to a conserved region of myosin-VI, which consist of three helices: MIU (Motif Interacting with Ubiquitin), a common linker helix (linker-alpha1) and an isoform-specific helix (linker-alpha2).


The actual alignment was detected with superfamily member pfam03285:

Pssm-ID: 480843  Cd Length: 301  Bit Score: 154.52  E-value: 2.02e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279   15 AEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLEDNIQRLEQEIQAL 94
Cdd:pfam03285    1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80

                           90       100
                   ....*....|....*....|...
gi 1847688279   95 ESEESQISAKEQIILEKLKETEK 117
Cdd:pfam03285   81 EEESSISAKKENLAEKLLEITVE 103
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 744-1021 1.69e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279  744 PQTDNPSEGREGVSKSFSDHGFYSPSSTLGD----SPSVDDPLEYQAGllVQNAIQQAIAEQVDKAEAHTSKEGSEQQEP 819
Cdd:pfam03154  110 PNSPSEGEGESSDGRSVNDEGSSDPKDIDQDnrstSPSIPSPQDNESD--SDSSAQQQILQTQPPVLQAQSGAASPPSPP 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279  820 EATVEEAGSQTPGSEKPQgmfAPPQVSSP-----------------VQEKRDILPKNLPAEDRALREKGPSQPP--TAAQ 880
Cdd:pfam03154  188 PPGTTQAATAGPTPSAPS---VPPQGSPAtsqppnqtqstaaphtlIQQTPTLHPQRLPSPHPPLQPMTQPPPPsqVSPQ 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279  881 PSGPVNMEETRPEGGYfskyseaaELRSTASLLatqESDVMVGPFKLRSRKQRTlsmieeeiRAAQEREEELKRQRQVRQ 960
Cdd:pfam03154  265 PLPQPSLHGQMPPMPH--------SLQTGPSHM---QHPVPPQPFPLTPQSSQS--------QVPPGPSPAAPGQSQQRI 325

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847688279  961 STPSPRAKNAPSLPSRTTCYKTAPGKIEKVKPPP-SPTTEGPSLQPDLAPEEAAGT---QRPKNL 1021
Cdd:pfam03154  326 HTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPtTPIPQLPNPQSHKHPPHLSGPspfQMNSNL 390
 
Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
15-117 2.02e-41

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 154.52  E-value: 2.02e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279   15 AEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLEDNIQRLEQEIQAL 94
Cdd:pfam03285    1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80

                           90       100
                   ....*....|....*....|...
gi 1847688279   95 ESEESQISAKEQIILEKLKETEK 117
Cdd:pfam03285   81 EEESSISAKKENLAEKLLEITVE 103
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 4-129 1.19e-05

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: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    4 AELHKERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKwllqgvpAGTAEEEEARRRQSEEdefkVKQLEDN 83
Cdd:COG1196    249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-------AELARLEQDIARLEER----RRELEER 317

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1847688279   84 IQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFSTA 129
Cdd:COG1196    318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 1-146 2.81e-04

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: 44.24  E-value: 2.81e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279     1 MAEAELHKERLQAIaekRKRQTEIEGKRRQLDEQVLLLQHSKSKVLrekWLLQGVPAGTAEEEEARRRQSEEDEFKVKQL 80
Cdd:smart00787  164 MKELELLNSIKPKL---RDRKDALEEELRQLKQLEDELEDCDPTEL---DRAKEKLKKLLQEIMIKVKKLEELEEELQEL 237

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1847688279    81 EDNIQRLEQEIQALeseESQISAKEQIILEKLKETEKSFKDLQKSFSTADGASGWSTVLLQGDELT 146
Cdd:smart00787  238 ESKIEDLTNKKSEL---NTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLTGWKITKLSGNTLS 300
PRK12704 PRK12704
phosphodiesterase; Provisional
 2-114 7.05e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 7.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    2 AEAELHKERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKV-LREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQL 80
Cdd:PRK12704    62 AKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLeKREEELEKKEKELEQKQQELEKKEEELEELIEEQL 141

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1847688279   81 edniQRLEqEIQALESEEsqisAKeQIILEKLKE 114
Cdd:PRK12704   142 ----QELE-RISGLTAEE----AK-EILLEKVEE 165
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 9-129 1.30e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    9 ERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLEDNIQRLE 88
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1847688279   89 QEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFSTA 129
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 744-1021 1.69e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279  744 PQTDNPSEGREGVSKSFSDHGFYSPSSTLGD----SPSVDDPLEYQAGllVQNAIQQAIAEQVDKAEAHTSKEGSEQQEP 819
Cdd:pfam03154  110 PNSPSEGEGESSDGRSVNDEGSSDPKDIDQDnrstSPSIPSPQDNESD--SDSSAQQQILQTQPPVLQAQSGAASPPSPP 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279  820 EATVEEAGSQTPGSEKPQgmfAPPQVSSP-----------------VQEKRDILPKNLPAEDRALREKGPSQPP--TAAQ 880
Cdd:pfam03154  188 PPGTTQAATAGPTPSAPS---VPPQGSPAtsqppnqtqstaaphtlIQQTPTLHPQRLPSPHPPLQPMTQPPPPsqVSPQ 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279  881 PSGPVNMEETRPEGGYfskyseaaELRSTASLLatqESDVMVGPFKLRSRKQRTlsmieeeiRAAQEREEELKRQRQVRQ 960
Cdd:pfam03154  265 PLPQPSLHGQMPPMPH--------SLQTGPSHM---QHPVPPQPFPLTPQSSQS--------QVPPGPSPAAPGQSQQRI 325

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847688279  961 STPSPRAKNAPSLPSRTTCYKTAPGKIEKVKPPP-SPTTEGPSLQPDLAPEEAAGT---QRPKNL 1021
Cdd:pfam03154  326 HTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPtTPIPQLPNPQSHKHPPHLSGPspfQMNSNL 390
PHA03247 PHA03247
large tegument protein UL36; Provisional
 819-1016 4.76e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 4.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279  819 PEATVEEAGSQTPGSEKPQGMFAPPQVSSPVQEKRDILPKNlPAEDRALREKGPSQPPTAAQPSGPVNMEETRPEGgyfs 898
Cdd:PHA03247  2775 PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA-AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS---- 2849

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279  899 kyseaaelrstaslLATQESDVMVGPFKLR--SRKQRTLSMIEEEIRAAQEREEELKRQRQ-VRQSTPSPRAKNAPSLPS 975
Cdd:PHA03247  2850 --------------LPLGGSVAPGGDVRRRppSRSPAAKPAAPARPPVRRLARPAVSRSTEsFALPPDQPERPPQPQAPP 2915

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1847688279  976 RTTCYKTAPGKIEKVKPPPSPTTEGPSLQPDLAPEEAAGTQ 1016
Cdd:PHA03247  2916 PPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS 2956
 
Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
15-117 2.02e-41

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 154.52  E-value: 2.02e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279   15 AEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLEDNIQRLEQEIQAL 94
Cdd:pfam03285    1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80

                           90       100
                   ....*....|....*....|...
gi 1847688279   95 ESEESQISAKEQIILEKLKETEK 117
Cdd:pfam03285   81 EEESSISAKKENLAEKLLEITVE 103
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 4-129 1.19e-05

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: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    4 AELHKERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKwllqgvpAGTAEEEEARRRQSEEdefkVKQLEDN 83
Cdd:COG1196    249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-------AELARLEQDIARLEER----RRELEER 317

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1847688279   84 IQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFSTA 129
Cdd:COG1196    318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
4-186 2.37e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    4 AELHKERLQA---IAEKRKRQTEIEGKRRQLDEQVLLLQhsksKVLREKWLLQGVPAgtAEEE----EARRRQSEEDEFK 76
Cdd:COG4913    613 AALEAELAELeeeLAEAEERLEALEAELDALQERREALQ----RLAEYSWDEIDVAS--AEREiaelEAELERLDASSDD 686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279   77 VKQLEDNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFSTAdGASGWSTVLLQGDELTADPIGTNADM 156
Cdd:COG4913    687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA-EDLARLELRALLEERFAAALGDAVER 765

                          170       180       190
                   ....*....|....*....|....*....|
gi 1847688279  157 AIQKppQLSEDANQLRSKQDNCGDsRLEPA 186
Cdd:COG4913    766 ELRE--NLEERIDALRARLNRAEE-ELERA 792
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
8-114 3.14e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 3.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    8 KERLQA-IAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEF----KVKQLED 82
Cdd:COG4913    340 LEQLEReIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAeaeaALRDLRR 419

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1847688279   83 NIQRLEQEIQALESEESQISAKEQIILEKLKE 114
Cdd:COG4913    420 ELRELEAEIASLERRKSNIPARLLALRDALAE 451
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
9-117 1.16e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    9 ERLQAIAEKRKRQTEIEGKRRQLDEQvlLLQHSKSkvlREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLEDNIQRLE 88
Cdd:COG4717    385 EELRAALEQAEEYQELKEELEELEEQ--LEELLGE---LEELLEALDEEELEEELEELEEELEELEEELEELREELAELE 459

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1847688279   89 QEIQALESEE--SQISAKEQIILEKLKETEK 117
Cdd:COG4717    460 AELEQLEEDGelAELLQELEELKAELRELAE 490
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-124 2.30e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    2 AEAELHKERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLE 81
Cdd:COG1196    327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1847688279   82 DNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQK 124
Cdd:COG1196    407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 3-123 2.79e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.11  E-value: 2.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    3 EAELHKERLQAIAEKRKRQtEIEGKRRQLDEQVL------LLQHSKSKVLREKWLLQgvpAGTAEEEEARRRQSEEDEFK 76
Cdd:pfam17380  469 EEERKRKKLELEKEKRDRK-RAEEQRRKILEKELeerkqaMIEEERKRKLLEKEMEE---RQKAIYEEERRREAEEERRK 544

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1847688279   77 VKQLEDNiQRLEQEIQALESEESQISA--KEQIILEKLKETEKSFKDLQ 123
Cdd:pfam17380  545 QQEMEER-RRIQEQMRKATEERSRLEAmeREREMMRQIVESEKARAEYE 592
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 1-146 2.81e-04

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: 44.24  E-value: 2.81e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279     1 MAEAELHKERLQAIaekRKRQTEIEGKRRQLDEQVLLLQHSKSKVLrekWLLQGVPAGTAEEEEARRRQSEEDEFKVKQL 80
Cdd:smart00787  164 MKELELLNSIKPKL---RDRKDALEEELRQLKQLEDELEDCDPTEL---DRAKEKLKKLLQEIMIKVKKLEELEEELQEL 237

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1847688279    81 EDNIQRLEQEIQALeseESQISAKEQIILEKLKETEKSFKDLQKSFSTADGASGWSTVLLQGDELT 146
Cdd:smart00787  238 ESKIEDLTNKKSEL---NTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLTGWKITKLSGNTLS 300
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1-124 4.70e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 4.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    1 MAEAELHKERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQL 80
Cdd:COG4717    118 LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1847688279   81 EDNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQK 124
Cdd:COG4717    198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
PRK12704 PRK12704
phosphodiesterase; Provisional
 2-114 7.05e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 7.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    2 AEAELHKERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKV-LREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQL 80
Cdd:PRK12704    62 AKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLeKREEELEKKEKELEQKQQELEKKEEELEELIEEQL 141

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1847688279   81 edniQRLEqEIQALESEEsqisAKeQIILEKLKE 114
Cdd:PRK12704   142 ----QELE-RISGLTAEE----AK-EILLEKVEE 165
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 9-129 1.30e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    9 ERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLEDNIQRLE 88
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1847688279   89 QEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFSTA 129
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-124 1.30e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    3 EAELHKERlqaIAEKRKRQTEIEGKRRQLDEQVLLLQH------SKSKVLREKwlLQGVPAGTAEEEEARRRQSEEDEFK 76
Cdd:PRK03918   232 ELEELKEE---IEELEKELESLEGSKRKLEEKIRELEErieelkKEIEELEEK--VKELKELKEKAEEYIKLSEFYEEYL 306

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1847688279   77 VK--QLEDNIQRLEQEIQALESEESQISAKEqiilEKLKETEKSFKDLQK 124
Cdd:PRK03918   307 DElrEIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEK 352
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 744-1021 1.69e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279  744 PQTDNPSEGREGVSKSFSDHGFYSPSSTLGD----SPSVDDPLEYQAGllVQNAIQQAIAEQVDKAEAHTSKEGSEQQEP 819
Cdd:pfam03154  110 PNSPSEGEGESSDGRSVNDEGSSDPKDIDQDnrstSPSIPSPQDNESD--SDSSAQQQILQTQPPVLQAQSGAASPPSPP 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279  820 EATVEEAGSQTPGSEKPQgmfAPPQVSSP-----------------VQEKRDILPKNLPAEDRALREKGPSQPP--TAAQ 880
Cdd:pfam03154  188 PPGTTQAATAGPTPSAPS---VPPQGSPAtsqppnqtqstaaphtlIQQTPTLHPQRLPSPHPPLQPMTQPPPPsqVSPQ 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279  881 PSGPVNMEETRPEGGYfskyseaaELRSTASLLatqESDVMVGPFKLRSRKQRTlsmieeeiRAAQEREEELKRQRQVRQ 960
Cdd:pfam03154  265 PLPQPSLHGQMPPMPH--------SLQTGPSHM---QHPVPPQPFPLTPQSSQS--------QVPPGPSPAAPGQSQQRI 325

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847688279  961 STPSPRAKNAPSLPSRTTCYKTAPGKIEKVKPPP-SPTTEGPSLQPDLAPEEAAGT---QRPKNL 1021
Cdd:pfam03154  326 HTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPtTPIPQLPNPQSHKHPPHLSGPspfQMNSNL 390
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-95 2.49e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    2 AEAELHKERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLE 81
Cdd:COG1196    687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766

                           90
                   ....*....|....
gi 1847688279   82 DNIQRLEQEIQALE 95
Cdd:COG1196    767 RELERLEREIEALG 780
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1-111 3.18e-03

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 39.26  E-value: 3.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    1 MAEAELHKERLQAIAEKRKRQTEIEGKRRQLDEqvLLLQHSKskvlrekwllqgvpagtaEEEEARRRQSEEdefKVKQL 80
Cdd:pfam15346   53 QVLEELEREREAELEEERRKEEEERKKREELER--ILEENNR------------------KIEEAQRKEAEE---RLAML 109

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1847688279   81 EDnIQRLEQEIQALESEESQISAKEQ-IILEK 111
Cdd:pfam15346  110 EE-QRRMKEERQRREKEEEEREKREQqKILNK 140
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 4-124 3.78e-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: 40.29  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    4 AELHKERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVP------AGTAEEEEARRRQSEEdEFKV 77
Cdd:COG1579     34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyeALQKEIESLKRRISDL-EDEI 112

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1847688279   78 KQLEDNIQRLEQEIQALESE----ESQISAKEQIILEKLKETEKSFKDLQK 124
Cdd:COG1579    113 LELMERIEELEEELAELEAElaelEAELEEKKAELDEELAELEAELEELEA 163
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
8-127 4.21e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 4.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    8 KERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREkwlLQGVPAGTAEEEEARRRQSEE--DEF-KVKQLEDNI 84
Cdd:PRK03918   538 KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE---LEELGFESVEELEERLKELEPfyNEYlELKDAEKEL 614

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1847688279   85 QRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFS 127
Cdd:PRK03918   615 EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
PHA03247 PHA03247
large tegument protein UL36; Provisional
 819-1016 4.76e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 4.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279  819 PEATVEEAGSQTPGSEKPQGMFAPPQVSSPVQEKRDILPKNlPAEDRALREKGPSQPPTAAQPSGPVNMEETRPEGgyfs 898
Cdd:PHA03247  2775 PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA-AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS---- 2849

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279  899 kyseaaelrstaslLATQESDVMVGPFKLR--SRKQRTLSMIEEEIRAAQEREEELKRQRQ-VRQSTPSPRAKNAPSLPS 975
Cdd:PHA03247  2850 --------------LPLGGSVAPGGDVRRRppSRSPAAKPAAPARPPVRRLARPAVSRSTEsFALPPDQPERPPQPQAPP 2915

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1847688279  976 RTTCYKTAPGKIEKVKPPPSPTTEGPSLQPDLAPEEAAGTQ 1016
Cdd:PHA03247  2916 PPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS 2956
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-129 6.01e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 6.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    2 AEAELHKERLQaIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLE 81
Cdd:COG1196    265 LEAELEELRLE-LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1847688279   82 DNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFSTA 129
Cdd:COG1196    344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-114 7.93e-03

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: 40.43  E-value: 7.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    2 AEAELHKERlQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSkskvlREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLE 81
Cdd:TIGR02168  377 LEEQLETLR-SKVAQLELQIASLNNEIERLEARLERLEDR-----RERLQQEIEELLKKLEEAELKELQAELEELEEELE 450

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1847688279   82 DNIQRLEQEIQALESEESQISAKEQIILEKLKE 114
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQALDAAERE 483
PRK12704 PRK12704
phosphodiesterase; Provisional
 60-124 9.70e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 9.70e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1847688279   60 AEEEEARRRQSEEDEFKVK---------QLEDNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQK 124
Cdd:PRK12704    62 AKEEIHKLRNEFEKELRERrnelqklekRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-129 9.71e-03

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: 40.04  E-value: 9.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847688279    2 AEAELHkERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLE 81
Cdd:TIGR02168  237 LREELE-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1847688279   82 DNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFSTA 129
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH