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Conserved domains on  [gi|1847915475|ref|NP_001371086|]
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paralemmin-2 isoform 8 [Mus musculus]

Protein Classification

Graphical summary

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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 ...
 17-119 2.19e-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: 2.19e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475   17 AEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLEDNIQRLEQEIQAL 96
Cdd:pfam03285    1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80

                           90       100
                   ....*....|....*....|...
gi 1847915475   97 ESEESQISAKEQIILEKLKETEK 119
Cdd:pfam03285   81 EEESSISAKKENLAEKLLEITVE 103
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 746-1023 1.66e-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: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475  746 PQTDNPSEGREGVSKSFSDHGFYSPSSTLGD----SPSVDDPLEYQAGllVQNAIQQAIAEQVDKAEAHTSKEGSEQQEP 821
Cdd:pfam03154  110 PNSPSEGEGESSDGRSVNDEGSSDPKDIDQDnrstSPSIPSPQDNESD--SDSSAQQQILQTQPPVLQAQSGAASPPSPP 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475  822 EATVEEAGSQTPGSEKPQgmfAPPQVSSP-----------------VQEKRDILPKNLPAEDRALREKGPSQPP--TAAQ 882
Cdd:pfam03154  188 PPGTTQAATAGPTPSAPS---VPPQGSPAtsqppnqtqstaaphtlIQQTPTLHPQRLPSPHPPLQPMTQPPPPsqVSPQ 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475  883 PSGPVNMEETRPEGGYfskyseaaELRSTASLLatqESDVMVGPFKLRSRKQRTlsmieeeiRAAQEREEELKRQRQVRQ 962
Cdd:pfam03154  265 PLPQPSLHGQMPPMPH--------SLQTGPSHM---QHPVPPQPFPLTPQSSQS--------QVPPGPSPAAPGQSQQRI 325

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847915475  963 STPSPRAKNAPSLPSRTTCYKTAPGKIEKVKPPP-SPTTEGPSLQPDLAPEEAAGT---QRPKNL 1023
Cdd:pfam03154  326 HTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPtTPIPQLPNPQSHKHPPHLSGPspfQMNSNL 390
 
Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
17-119 2.19e-41

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 154.52  E-value: 2.19e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475   17 AEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLEDNIQRLEQEIQAL 96
Cdd:pfam03285    1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80

                           90       100
                   ....*....|....*....|...
gi 1847915475   97 ESEESQISAKEQIILEKLKETEK 119
Cdd:pfam03285   81 EEESSISAKKENLAEKLLEITVE 103
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-131 1.02e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    2 EMAEAELHKERLQAiaEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKwllqgvpAGTAEEEEARRRQSEEdefkVKQ 81
Cdd:COG1196    247 ELEELEAELEELEA--ELAELEAELEELRLELEELELELEEAQAEEYELL-------AELARLEQDIARLEER----RRE 313

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1847915475   82 LEDNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFSTA 131
Cdd:COG1196    314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 3-148 3.02e-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: 3.02e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475     3 MAEAELHKERLQAIaekRKRQTEIEGKRRQLDEQVLLLQHSKSKVLrekWLLQGVPAGTAEEEEARRRQSEEDEFKVKQL 82
Cdd:smart00787  164 MKELELLNSIKPKL---RDRKDALEEELRQLKQLEDELEDCDPTEL---DRAKEKLKKLLQEIMIKVKKLEELEEELQEL 237

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1847915475    83 EDNIQRLEQEIQALeseESQISAKEQIILEKLKETEKSFKDLQKSFSTADGASGWSTVLLQGDELT 148
Cdd:smart00787  238 ESKIEDLTNKKSEL---NTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLTGWKITKLSGNTLS 300
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1-126 5.99e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 5.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    1 MEMAEAELH--KERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQH------SKSKVLREKwlLQGVPAGTAEEEEARRRQS 72
Cdd:PRK03918   223 LEKLEKEVKelEELKEEIEELEKELESLEGSKRKLEEKIRELEErieelkKEIEELEEK--VKELKELKEKAEEYIKLSE 300

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1847915475   73 EEDEFKVK--QLEDNIQRLEQEIQALESEESQISAKEqiilEKLKETEKSFKDLQK 126
Cdd:PRK03918   301 FYEEYLDElrEIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEK 352
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 4-125 9.17e-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: 43.51  E-value: 9.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    4 AEAELHKERLQAIAEKRKR-QTEIEGKRRQLDEQVLLLQHSKSKVLRekwlLQGVPAGTAEEEEARRRQSEEDEFKVKQL 82
Cdd:TIGR02168  302 QQKQILRERLANLERQLEElEAQLEELESKLDELAEELAELEEKLEE----LKEELESLEAELEELEAELEELESRLEEL 377

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1847915475   83 EDNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQ 125
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 746-1023 1.66e-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: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475  746 PQTDNPSEGREGVSKSFSDHGFYSPSSTLGD----SPSVDDPLEYQAGllVQNAIQQAIAEQVDKAEAHTSKEGSEQQEP 821
Cdd:pfam03154  110 PNSPSEGEGESSDGRSVNDEGSSDPKDIDQDnrstSPSIPSPQDNESD--SDSSAQQQILQTQPPVLQAQSGAASPPSPP 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475  822 EATVEEAGSQTPGSEKPQgmfAPPQVSSP-----------------VQEKRDILPKNLPAEDRALREKGPSQPP--TAAQ 882
Cdd:pfam03154  188 PPGTTQAATAGPTPSAPS---VPPQGSPAtsqppnqtqstaaphtlIQQTPTLHPQRLPSPHPPLQPMTQPPPPsqVSPQ 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475  883 PSGPVNMEETRPEGGYfskyseaaELRSTASLLatqESDVMVGPFKLRSRKQRTlsmieeeiRAAQEREEELKRQRQVRQ 962
Cdd:pfam03154  265 PLPQPSLHGQMPPMPH--------SLQTGPSHM---QHPVPPQPFPLTPQSSQS--------QVPPGPSPAAPGQSQQRI 325

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847915475  963 STPSPRAKNAPSLPSRTTCYKTAPGKIEKVKPPP-SPTTEGPSLQPDLAPEEAAGT---QRPKNL 1023
Cdd:pfam03154  326 HTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPtTPIPQLPNPQSHKHPPHLSGPspfQMNSNL 390
PHA03247 PHA03247
large tegument protein UL36; Provisional
 821-1018 4.46e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 4.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475  821 PEATVEEAGSQTPGSEKPQGMFAPPQVSSPVQEKRDILPKNlPAEDRALREKGPSQPPTAAQPSGPVNMEETRPEGgyfs 900
Cdd:PHA03247  2775 PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA-AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS---- 2849

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475  901 kyseaaelrstaslLATQESDVMVGPFKLR--SRKQRTLSMIEEEIRAAQEREEELKRQRQ-VRQSTPSPRAKNAPSLPS 977
Cdd:PHA03247  2850 --------------LPLGGSVAPGGDVRRRppSRSPAAKPAAPARPPVRRLARPAVSRSTEsFALPPDQPERPPQPQAPP 2915

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1847915475  978 RTTCYKTAPGKIEKVKPPPSPTTEGPSLQPDLAPEEAAGTQ 1018
Cdd:PHA03247  2916 PPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS 2956
 
Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
17-119 2.19e-41

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 154.52  E-value: 2.19e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475   17 AEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLEDNIQRLEQEIQAL 96
Cdd:pfam03285    1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80

                           90       100
                   ....*....|....*....|...
gi 1847915475   97 ESEESQISAKEQIILEKLKETEK 119
Cdd:pfam03285   81 EEESSISAKKENLAEKLLEITVE 103
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-131 1.02e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    2 EMAEAELHKERLQAiaEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKwllqgvpAGTAEEEEARRRQSEEdefkVKQ 81
Cdd:COG1196    247 ELEELEAELEELEA--ELAELEAELEELRLELEELELELEEAQAEEYELL-------AELARLEQDIARLEER----RRE 313

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1847915475   82 LEDNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFSTA 131
Cdd:COG1196    314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-188 2.10e-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: 2.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    2 EMAEAELHKERlQAIAEKRKRQTEIEGKRRQLDEQVLLLQhsksKVLREKWLLQGVPAgtAEEE----EARRRQSEEDEF 77
Cdd:COG4913    613 AALEAELAELE-EELAEAEERLEALEAELDALQERREALQ----RLAEYSWDEIDVAS--AEREiaelEAELERLDASSD 685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475   78 KVKQLEDNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFSTAdGASGWSTVLLQGDELTADPIGTNAD 157
Cdd:COG4913    686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA-EDLARLELRALLEERFAAALGDAVE 764

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1847915475  158 MAIQKppQLSEDANQLRSKQDNCGDsRLEPA 188
Cdd:COG4913    765 RELRE--NLEERIDALRARLNRAEE-ELERA 792
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
10-116 3.15e-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: 3.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475   10 KERLQA-IAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEF----KVKQLED 84
Cdd:COG4913    340 LEQLEReIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAeaeaALRDLRR 419

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1847915475   85 NIQRLEQEIQALESEESQISAKEQIILEKLKE 116
Cdd:COG4913    420 ELRELEAEIASLERRKSNIPARLLALRDALAE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-126 1.02e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    2 EMAEAELHKERLQA-IAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVK 80
Cdd:COG1196    324 ELAELEEELEELEEeLEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1847915475   81 QLEDNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQK 126
Cdd:COG1196    404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
11-119 1.18e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475   11 ERLQAIAEKRKRQTEIEGKRRQLDEQvlLLQHSKSkvlREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLEDNIQRLE 90
Cdd:COG4717    385 EELRAALEQAEEYQELKEELEELEEQ--LEELLGE---LEELLEALDEEELEEELEELEEELEELEEELEELREELAELE 459

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1847915475   91 QEIQALESEE--SQISAKEQIILEKLKETEK 119
Cdd:COG4717    460 AELEQLEEDGelAELLQELEELKAELRELAE 490
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2-126 1.89e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    2 EMAEAELHKERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQ 81
Cdd:COG4717    117 ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD 196

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1847915475   82 LEDNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQK 126
Cdd:COG4717    197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 3-148 3.02e-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: 3.02e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475     3 MAEAELHKERLQAIaekRKRQTEIEGKRRQLDEQVLLLQHSKSKVLrekWLLQGVPAGTAEEEEARRRQSEEDEFKVKQL 82
Cdd:smart00787  164 MKELELLNSIKPKL---RDRKDALEEELRQLKQLEDELEDCDPTEL---DRAKEKLKKLLQEIMIKVKKLEELEEELQEL 237

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1847915475    83 EDNIQRLEQEIQALeseESQISAKEQIILEKLKETEKSFKDLQKSFSTADGASGWSTVLLQGDELT 148
Cdd:smart00787  238 ESKIEDLTNKKSEL---NTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLTGWKITKLSGNTLS 300
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 5-125 3.31e-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: 44.73  E-value: 3.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    5 EAELHKERLQAIAEKRKRQtEIEGKRRQLDEQVL------LLQHSKSKVLREKWLLQgvpAGTAEEEEARRRQSEEDEFK 78
Cdd:pfam17380  469 EEERKRKKLELEKEKRDRK-RAEEQRRKILEKELeerkqaMIEEERKRKLLEKEMEE---RQKAIYEEERRREAEEERRK 544

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1847915475   79 VKQLEDNiQRLEQEIQALESEESQISA--KEQIILEKLKETEKSFKDLQ 125
Cdd:pfam17380  545 QQEMEER-RRIQEQMRKATEERSRLEAmeREREMMRQIVESEKARAEYE 592
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1-126 5.99e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 5.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    1 MEMAEAELH--KERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQH------SKSKVLREKwlLQGVPAGTAEEEEARRRQS 72
Cdd:PRK03918   223 LEKLEKEVKelEELKEEIEELEKELESLEGSKRKLEEKIRELEErieelkKEIEELEEK--VKELKELKEKAEEYIKLSE 300

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1847915475   73 EEDEFKVK--QLEDNIQRLEQEIQALESEESQISAKEqiilEKLKETEKSFKDLQK 126
Cdd:PRK03918   301 FYEEYLDElrEIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEK 352
PRK12704 PRK12704
phosphodiesterase; Provisional
 4-116 7.25e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 7.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    4 AEAELHKERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKV-LREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQL 82
Cdd:PRK12704    62 AKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLeKREEELEKKEKELEQKQQELEKKEEELEELIEEQL 141

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1847915475   83 edniQRLEqEIQALESEEsqisAKeQIILEKLKE 116
Cdd:PRK12704   142 ----QELE-RISGLTAEE----AK-EILLEKVEE 165
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 4-125 9.17e-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: 43.51  E-value: 9.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    4 AEAELHKERLQAIAEKRKR-QTEIEGKRRQLDEQVLLLQHSKSKVLRekwlLQGVPAGTAEEEEARRRQSEEDEFKVKQL 82
Cdd:TIGR02168  302 QQKQILRERLANLERQLEElEAQLEELESKLDELAEELAELEEKLEE----LKEELESLEAELEELEAELEELESRLEEL 377

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1847915475   83 EDNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQ 125
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 11-131 1.29e-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: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475   11 ERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLEDNIQRLE 90
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1847915475   91 QEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFSTA 131
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 746-1023 1.66e-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: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475  746 PQTDNPSEGREGVSKSFSDHGFYSPSSTLGD----SPSVDDPLEYQAGllVQNAIQQAIAEQVDKAEAHTSKEGSEQQEP 821
Cdd:pfam03154  110 PNSPSEGEGESSDGRSVNDEGSSDPKDIDQDnrstSPSIPSPQDNESD--SDSSAQQQILQTQPPVLQAQSGAASPPSPP 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475  822 EATVEEAGSQTPGSEKPQgmfAPPQVSSP-----------------VQEKRDILPKNLPAEDRALREKGPSQPP--TAAQ 882
Cdd:pfam03154  188 PPGTTQAATAGPTPSAPS---VPPQGSPAtsqppnqtqstaaphtlIQQTPTLHPQRLPSPHPPLQPMTQPPPPsqVSPQ 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475  883 PSGPVNMEETRPEGGYfskyseaaELRSTASLLatqESDVMVGPFKLRSRKQRTlsmieeeiRAAQEREEELKRQRQVRQ 962
Cdd:pfam03154  265 PLPQPSLHGQMPPMPH--------SLQTGPSHM---QHPVPPQPFPLTPQSSQS--------QVPPGPSPAAPGQSQQRI 325

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847915475  963 STPSPRAKNAPSLPSRTTCYKTAPGKIEKVKPPP-SPTTEGPSLQPDLAPEEAAGT---QRPKNL 1023
Cdd:pfam03154  326 HTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPtTPIPQLPNPQSHKHPPHLSGPspfQMNSNL 390
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 2-113 1.96e-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: 40.03  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    2 EMAEAELHKERLQAIAEKRKRQTEIEGKRRQLDEqvLLLQHSKskvlrekwllqgvpagtaEEEEARRRQSEEdefKVKQ 81
Cdd:pfam15346   52 KQVLEELEREREAELEEERRKEEEERKKREELER--ILEENNR------------------KIEEAQRKEAEE---RLAM 108

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1847915475   82 LEDnIQRLEQEIQALESEESQISAKEQ-IILEK 113
Cdd:pfam15346  109 LEE-QRRMKEERQRREKEEEEREKREQqKILNK 140
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 4-97 2.51e-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: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    4 AEAELHKERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLE 83
Cdd:COG1196    687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766

                           90
                   ....*....|....
gi 1847915475   84 DNIQRLEQEIQALE 97
Cdd:COG1196    767 RELERLEREIEALG 780
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-116 3.00e-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: 41.97  E-value: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    1 MEMAEAELHKERLQ---AIAEKRKRQTEIEGKRRQLDEQVLLLQHSkskvlREKWLLQGVPAGTAEEEEARRRQSEEDEF 77
Cdd:TIGR02168  370 LESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARLERLEDR-----RERLQQEIEELLKKLEEAELKELQAELEE 444

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1847915475   78 KVKQLEDNIQRLEQEIQALESEESQISAKEQIILEKLKE 116
Cdd:TIGR02168  445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 6-126 3.85e-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: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    6 AELHKERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVP------AGTAEEEEARRRQSEEdEFKV 79
Cdd:COG1579     34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyeALQKEIESLKRRISDL-EDEI 112

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1847915475   80 KQLEDNIQRLEQEIQALESE----ESQISAKEQIILEKLKETEKSFKDLQK 126
Cdd:COG1579    113 LELMERIEELEEELAELEAElaelEAELEEKKAELDEELAELEAELEELEA 163
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
10-129 4.33e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475   10 KERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREkwlLQGVPAGTAEEEEARRRQSEE--DEF-KVKQLEDNI 86
Cdd:PRK03918   538 KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE---LEELGFESVEELEERLKELEPfyNEYlELKDAEKEL 614

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1847915475   87 QRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFS 129
Cdd:PRK03918   615 EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
PHA03247 PHA03247
large tegument protein UL36; Provisional
 821-1018 4.46e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 4.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475  821 PEATVEEAGSQTPGSEKPQGMFAPPQVSSPVQEKRDILPKNlPAEDRALREKGPSQPPTAAQPSGPVNMEETRPEGgyfs 900
Cdd:PHA03247  2775 PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA-AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS---- 2849

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475  901 kyseaaelrstaslLATQESDVMVGPFKLR--SRKQRTLSMIEEEIRAAQEREEELKRQRQ-VRQSTPSPRAKNAPSLPS 977
Cdd:PHA03247  2850 --------------LPLGGSVAPGGDVRRRppSRSPAAKPAAPARPPVRRLARPAVSRSTEsFALPPDQPERPPQPQAPP 2915

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1847915475  978 RTTCYKTAPGKIEKVKPPPSPTTEGPSLQPDLAPEEAAGTQ 1018
Cdd:PHA03247  2916 PPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS 2956
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-131 4.79e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 4.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    2 EMAEAELHKERL-QAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVK 80
Cdd:COG1196    261 ELAELEAELEELrLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1847915475   81 QLEDNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFSTA 131
Cdd:COG1196    341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-131 8.01e-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: 8.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    1 MEMAEAELHkERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVK 80
Cdd:TIGR02168  234 LEELREELE-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1847915475   81 QLEDNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFSTA 131
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-119 8.10e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 8.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847915475    2 EMAEAELHKERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQ 81
Cdd:COG1196    315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1847915475   82 LEDNIQRLEQEIQALESEESQISAKEQIILEKLKETEK 119
Cdd:COG1196    395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
PRK12704 PRK12704
phosphodiesterase; Provisional
 62-126 9.89e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 9.89e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1847915475   62 AEEEEARRRQSEEDEFKVK---------QLEDNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQK 126
Cdd:PRK12704    62 AKEEIHKLRNEFEKELRERrnelqklekRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135
 
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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