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Conserved domains on  [gi|1720380201|ref|XP_030103753|]
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apoptotic chromatin condensation inducer in the nucleus isoform X3 [Mus musculus]

Protein Classification

RRM_ACINU and RSB_motif domain-containing protein( domain architecture ID 11271100)

protein containing domains SAP, RRM_ACINU, and RSB_motif

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RRM_ACINU cd12432
RNA recognition motif (RRM) found in apoptotic chromatin condensation inducer in the nucleus ...
969-1055 2.36e-48

RNA recognition motif (RRM) found in apoptotic chromatin condensation inducer in the nucleus (acinus) and similar proteins; This subfamily corresponds to the RRM of Acinus, a caspase-3-activated nuclear factor that induces apoptotic chromatin condensation after cleavage by caspase-3 without inducing DNA fragmentation. It is essential for apoptotic chromatin condensation and may also participate in nuclear structural changes occurring in normal cells. Acinus contains a P-loop motif and an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), which indicates Acinus might have ATPase and DNA/RNA-binding activity.


:

Pssm-ID: 409866 [Multi-domain]  Cd Length: 90  Bit Score: 166.61  E-value: 2.36e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  969 SNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQD 1048
Cdd:cd12432      1 SRILHIDNLVRPFTLGQLKELLSETGTGVIEGFWMDKIKSHCYVTYSSEEEAVATREALHGVVWPSSNGKRLKVEFVTEE 80

                   ....*..
gi 1720380201 1049 ELDYHRG 1055
Cdd:cd12432     81 ELEELIE 87
RSB_motif pfam16294
RNSP1-SAP18 binding (RSB) motif; The RSB motif on the Acinus protein is the core around which ...
1164-1198 1.33e-14

RNSP1-SAP18 binding (RSB) motif; The RSB motif on the Acinus protein is the core around which the ASAP complex is built. The apoptosis and splicing-associated protein complex, ASAP, is made up of three proteins, SAP18 (Sin3-associated protein of 18 kDa), RNA-binding protein S1 (RNPS1) and apoptotic chromatin inducer in the nucleus (Acinus). The ASAP complex appears to be an assembly of proteins at the interface between transcription, splicing and NMD, acting as a hub in the network of protein-interactions that regulate gene-expression.


:

Pssm-ID: 465085  Cd Length: 91  Bit Score: 70.53  E-value: 1.33e-14
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720380201 1164 PPAKLLDDLFRKTKAAPCIYWLPLTESQIVQKEAE 1198
Cdd:pfam16294   50 PPAKLLDDLFRKTKATPCIYWLPLTPEQIAEKEAQ 84
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
72-106 7.90e-07

Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;


:

Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 46.71  E-value: 7.90e-07
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1720380201    72 LQALRVTDLKAALEQRGLAKSGQKSALVKRLKGAL 106
Cdd:smart00513    1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
PTZ00121 super family cl31754
MAEBL; Provisional
81-376 3.86e-04

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 3.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201   81 KAALEQRGLAKSGQKSALVKRLKGALMLENLQKHSTPHAAFQPNSQIGEEMSQNSFIKQYLEKQQELLRQRLEREAREAA 160
Cdd:PTZ00121  1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  161 ELEGKSssfsEEKGESDDEKPRKGERRSSRVRQAKSKLPEYSQTAEEEEDQETPSRNLRVRADRNLKIEEEEEEEEEEED 240
Cdd:PTZ00121  1409 ELKKAA----AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK 1484
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  241 DDDEEEEEVDEAQKSREAEAptlKQFEDEEGEERTRAKPEKVVDEKPLNIRSQEKGELEKGGRVTRSQEEARRSHLARQQ 320
Cdd:PTZ00121  1485 ADEAKKKAEEAKKKADEAKK---AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720380201  321 QEKETQIVSLPQEENEVKSSQSLEEKSQSPSPPPLPEDLEKAPVVLQPEQIVSEEE 376
Cdd:PTZ00121  1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
PDHac_trf_long super family cl36876
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
373-507 9.17e-03

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


The actual alignment was detected with superfamily member TIGR01348:

Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 40.24  E-value: 9.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  373 SEEETPPPLLTKEASSPPTHIQLQEEMEPVEGPAPPvliQLSPPNT-DAGAREPLASPHPAQLLRSLSPLSGT--TDTKA 449
Cdd:TIGR01348  191 VAGSTPATAPAPASAQPAAQSPAATQPEPAAAPAAA---KAQAPAPqQAGTQNPAKVDHAAPAVRRLAREFGVdlSAVKG 267
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720380201  450 ESPAGRVSDESVLPLAQKSSLPECSTQKGVESEREKSAPLPLTveEFAPAKGITEEPM 507
Cdd:TIGR01348  268 TGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPGALPWPNV--DFSKFGEVEEVDM 323
 
Name Accession Description Interval E-value
RRM_ACINU cd12432
RNA recognition motif (RRM) found in apoptotic chromatin condensation inducer in the nucleus ...
969-1055 2.36e-48

RNA recognition motif (RRM) found in apoptotic chromatin condensation inducer in the nucleus (acinus) and similar proteins; This subfamily corresponds to the RRM of Acinus, a caspase-3-activated nuclear factor that induces apoptotic chromatin condensation after cleavage by caspase-3 without inducing DNA fragmentation. It is essential for apoptotic chromatin condensation and may also participate in nuclear structural changes occurring in normal cells. Acinus contains a P-loop motif and an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), which indicates Acinus might have ATPase and DNA/RNA-binding activity.


Pssm-ID: 409866 [Multi-domain]  Cd Length: 90  Bit Score: 166.61  E-value: 2.36e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  969 SNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQD 1048
Cdd:cd12432      1 SRILHIDNLVRPFTLGQLKELLSETGTGVIEGFWMDKIKSHCYVTYSSEEEAVATREALHGVVWPSSNGKRLKVEFVTEE 80

                   ....*..
gi 1720380201 1049 ELDYHRG 1055
Cdd:cd12432     81 ELEELIE 87
RSB_motif pfam16294
RNSP1-SAP18 binding (RSB) motif; The RSB motif on the Acinus protein is the core around which ...
1164-1198 1.33e-14

RNSP1-SAP18 binding (RSB) motif; The RSB motif on the Acinus protein is the core around which the ASAP complex is built. The apoptosis and splicing-associated protein complex, ASAP, is made up of three proteins, SAP18 (Sin3-associated protein of 18 kDa), RNA-binding protein S1 (RNPS1) and apoptotic chromatin inducer in the nucleus (Acinus). The ASAP complex appears to be an assembly of proteins at the interface between transcription, splicing and NMD, acting as a hub in the network of protein-interactions that regulate gene-expression.


Pssm-ID: 465085  Cd Length: 91  Bit Score: 70.53  E-value: 1.33e-14
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720380201 1164 PPAKLLDDLFRKTKAAPCIYWLPLTESQIVQKEAE 1198
Cdd:pfam16294   50 PPAKLLDDLFRKTKATPCIYWLPLTPEQIAEKEAQ 84
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
72-106 7.90e-07

Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 46.71  E-value: 7.90e-07
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1720380201    72 LQALRVTDLKAALEQRGLAKSGQKSALVKRLKGAL 106
Cdd:smart00513    1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
72-106 2.39e-06

SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins.


Pssm-ID: 460424 [Multi-domain]  Cd Length: 35  Bit Score: 45.08  E-value: 2.39e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720380201   72 LQALRVTDLKAALEQRGLAKSGQKSALVKRLKGAL 106
Cdd:pfam02037    1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
PTZ00121 PTZ00121
MAEBL; Provisional
81-376 3.86e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 3.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201   81 KAALEQRGLAKSGQKSALVKRLKGALMLENLQKHSTPHAAFQPNSQIGEEMSQNSFIKQYLEKQQELLRQRLEREAREAA 160
Cdd:PTZ00121  1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  161 ELEGKSssfsEEKGESDDEKPRKGERRSSRVRQAKSKLPEYSQTAEEEEDQETPSRNLRVRADRNLKIEEEEEEEEEEED 240
Cdd:PTZ00121  1409 ELKKAA----AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK 1484
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  241 DDDEEEEEVDEAQKSREAEAptlKQFEDEEGEERTRAKPEKVVDEKPLNIRSQEKGELEKGGRVTRSQEEARRSHLARQQ 320
Cdd:PTZ00121  1485 ADEAKKKAEEAKKKADEAKK---AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720380201  321 QEKETQIVSLPQEENEVKSSQSLEEKSQSPSPPPLPEDLEKAPVVLQPEQIVSEEE 376
Cdd:PTZ00121  1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
129-412 2.72e-03

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: 42.03  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  129 EEMSQNSFIKQYLEKQQELLRQRLEREAREA--AELEGKSSSFSEEKG-----ESDDEKPRKGERRSS--RVRQAKSKLp 199
Cdd:pfam17380  294 EKMEQERLRQEKEEKAREVERRRKLEEAEKArqAEMDRQAAIYAEQERmamerERELERIRQEERKREleRIRQEEIAM- 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  200 EYSQTAEEEEDQ-ETPSRNLRVRADRNLKIEEEEEEEEEEEDDDDEEEEEVDEAQKSREAEAPTLKQFEDEEGEERTRAK 278
Cdd:pfam17380  373 EISRMRELERLQmERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVR 452
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  279 PEKVVDEKPLNI-------RSQEKGELEKGGRVTRSQEEARRSHLARQQQEKETQIVSLPQE----ENEVKSSQSL---- 343
Cdd:pfam17380  453 LEEQERQQQVERlrqqeeeRKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKrkllEKEMEERQKAiyee 532
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720380201  344 EEKSQSPSPPPLPEDLEKAPVVLQPEQIVSEEETPPPLLTKEASSPPTHIQLQEEMEPVEGPAPPVLIQ 412
Cdd:pfam17380  533 ERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIK 601
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
141-326 4.16e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 4.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  141 LEKQQELLRQRLEREAREAAELEGKSSSFSEEKGESDDEKPRKGERRSSRVRQAKSKLPEYSQTAEEEEDQETPSRNLRV 220
Cdd:COG1196    328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  221 RADRNLKIEEEEEEEeeeeddddeEEEEVDEAQKSREAEAPTLKQFEDEEGEERTRAKPEKVVDEKPLNIRSQEKGELEK 300
Cdd:COG1196    408 AEEALLERLERLEEE---------LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
                          170       180
                   ....*....|....*....|....*.
gi 1720380201  301 GGRVTRSQEEARRSHLARQQQEKETQ 326
Cdd:COG1196    479 LAELLEELAEAAARLLLLLEAEADYE 504
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
373-507 9.17e-03

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 40.24  E-value: 9.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  373 SEEETPPPLLTKEASSPPTHIQLQEEMEPVEGPAPPvliQLSPPNT-DAGAREPLASPHPAQLLRSLSPLSGT--TDTKA 449
Cdd:TIGR01348  191 VAGSTPATAPAPASAQPAAQSPAATQPEPAAAPAAA---KAQAPAPqQAGTQNPAKVDHAAPAVRRLAREFGVdlSAVKG 267
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720380201  450 ESPAGRVSDESVLPLAQKSSLPECSTQKGVESEREKSAPLPLTveEFAPAKGITEEPM 507
Cdd:TIGR01348  268 TGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPGALPWPNV--DFSKFGEVEEVDM 323
 
Name Accession Description Interval E-value
RRM_ACINU cd12432
RNA recognition motif (RRM) found in apoptotic chromatin condensation inducer in the nucleus ...
969-1055 2.36e-48

RNA recognition motif (RRM) found in apoptotic chromatin condensation inducer in the nucleus (acinus) and similar proteins; This subfamily corresponds to the RRM of Acinus, a caspase-3-activated nuclear factor that induces apoptotic chromatin condensation after cleavage by caspase-3 without inducing DNA fragmentation. It is essential for apoptotic chromatin condensation and may also participate in nuclear structural changes occurring in normal cells. Acinus contains a P-loop motif and an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), which indicates Acinus might have ATPase and DNA/RNA-binding activity.


Pssm-ID: 409866 [Multi-domain]  Cd Length: 90  Bit Score: 166.61  E-value: 2.36e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  969 SNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQD 1048
Cdd:cd12432      1 SRILHIDNLVRPFTLGQLKELLSETGTGVIEGFWMDKIKSHCYVTYSSEEEAVATREALHGVVWPSSNGKRLKVEFVTEE 80

                   ....*..
gi 1720380201 1049 ELDYHRG 1055
Cdd:cd12432     81 ELEELIE 87
RSB_motif pfam16294
RNSP1-SAP18 binding (RSB) motif; The RSB motif on the Acinus protein is the core around which ...
1164-1198 1.33e-14

RNSP1-SAP18 binding (RSB) motif; The RSB motif on the Acinus protein is the core around which the ASAP complex is built. The apoptosis and splicing-associated protein complex, ASAP, is made up of three proteins, SAP18 (Sin3-associated protein of 18 kDa), RNA-binding protein S1 (RNPS1) and apoptotic chromatin inducer in the nucleus (Acinus). The ASAP complex appears to be an assembly of proteins at the interface between transcription, splicing and NMD, acting as a hub in the network of protein-interactions that regulate gene-expression.


Pssm-ID: 465085  Cd Length: 91  Bit Score: 70.53  E-value: 1.33e-14
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720380201 1164 PPAKLLDDLFRKTKAAPCIYWLPLTESQIVQKEAE 1198
Cdd:pfam16294   50 PPAKLLDDLFRKTKATPCIYWLPLTPEQIAEKEAQ 84
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
72-106 7.90e-07

Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 46.71  E-value: 7.90e-07
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1720380201    72 LQALRVTDLKAALEQRGLAKSGQKSALVKRLKGAL 106
Cdd:smart00513    1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
72-106 2.39e-06

SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins.


Pssm-ID: 460424 [Multi-domain]  Cd Length: 35  Bit Score: 45.08  E-value: 2.39e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720380201   72 LQALRVTDLKAALEQRGLAKSGQKSALVKRLKGAL 106
Cdd:pfam02037    1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
972-1031 3.79e-04

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).


Pssm-ID: 409669 [Multi-domain]  Cd Length: 72  Bit Score: 39.96  E-value: 3.79e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720380201  972 VHISNLVRPFTLGQLKELLGRTGTlVEEAFWID----KIKSHCFVTYSTVEEAVATRTALHGVK 1031
Cdd:cd00590      1 LFVGNLPPDTTEEDLRELFSKFGE-VVSVRIVRdrdgKSKGFAFVEFESPEDAEKALEALNGTE 63
PTZ00121 PTZ00121
MAEBL; Provisional
81-376 3.86e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 3.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201   81 KAALEQRGLAKSGQKSALVKRLKGALMLENLQKHSTPHAAFQPNSQIGEEMSQNSFIKQYLEKQQELLRQRLEREAREAA 160
Cdd:PTZ00121  1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  161 ELEGKSssfsEEKGESDDEKPRKGERRSSRVRQAKSKLPEYSQTAEEEEDQETPSRNLRVRADRNLKIEEEEEEEEEEED 240
Cdd:PTZ00121  1409 ELKKAA----AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK 1484
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  241 DDDEEEEEVDEAQKSREAEAptlKQFEDEEGEERTRAKPEKVVDEKPLNIRSQEKGELEKGGRVTRSQEEARRSHLARQQ 320
Cdd:PTZ00121  1485 ADEAKKKAEEAKKKADEAKK---AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720380201  321 QEKETQIVSLPQEENEVKSSQSLEEKSQSPSPPPLPEDLEKAPVVLQPEQIVSEEE 376
Cdd:PTZ00121  1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
75-209 5.00e-04

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 44.44  E-value: 5.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201   75 LRVTDLKAALEQRGLAKSGQKSALVKRLKGALMLENLQKHSTPHAAFQPNSQIGE-EMSQNSFIKQYLEKQQELLRQRLE 153
Cdd:PLN03124     5 LKVDELRAALAKRGLDTTGLKAALVRRLDDAIAEDAKTASKSGTKSSAGRKKRRErQDDGDDEPVSPKRIAIDEVKGMTV 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  154 REAREAAELEGKSSSFSE----EKGESDDEKPRKgeRRSSRVRQAKSKLPEYSQTAEEEE 209
Cdd:PLN03124    85 RELREAASERGLATTGRKkdllERLCAALESDVK--VGSANGTGEDEKEKGGDEEREKEE 142
PTZ00121 PTZ00121
MAEBL; Provisional
142-385 6.57e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 6.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  142 EKQQELLRQRLErEAREAAELEGKSssfsEEKGESDDEKPRKGERRssRVRQAKSKLPEySQTAEEEEDQETPSRnlrvR 221
Cdd:PTZ00121  1417 KKKADEAKKKAE-EKKKADEAKKKA----EEAKKADEAKKKAEEAK--KAEEAKKKAEE-AKKADEAKKKAEEAK----K 1484
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  222 ADRNLKIEEEEEEEEEEEDDDDEEEEEVDEAQKSREA-EAPTLKQFEDEEGEERTRAKPEKVVDEKPLNIRSQEKGELEK 300
Cdd:PTZ00121  1485 ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAkKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK 1564
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  301 GGRVTRSQEE-----ARRSHLARQQQEKETQIV-SLPQEENEVKSSQSLEEKSQSPSPPPLPEDLEKAPVVLQPEQIVSE 374
Cdd:PTZ00121  1565 KAEEAKKAEEdknmaLRKAEEAKKAEEARIEEVmKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
                          250
                   ....*....|.
gi 1720380201  375 EETPPPLLTKE 385
Cdd:PTZ00121  1645 EKKKAEELKKA 1655
RRM_ALKBH8 cd12431
RNA recognition motif (RRM) found in alkylated DNA repair protein alkB homolog 8 (ALKBH8) and ...
969-1047 8.05e-04

RNA recognition motif (RRM) found in alkylated DNA repair protein alkB homolog 8 (ALKBH8) and similar proteins; This subfamily corresponds to the RRM of ALKBH8, also termed alpha-ketoglutarate-dependent dioxygenase ABH8, or S-adenosyl-L-methionine-dependent tRNA methyltransferase ABH8, expressed in various types of human cancers. It is essential in urothelial carcinoma cell survival mediated by NOX-1-dependent ROS signals. ALKBH8 has also been identified as a tRNA methyltransferase that catalyzes methylation of tRNA to yield 5-methylcarboxymethyl uridine (mcm5U) at the wobble position of the anticodon loop. Thus, ALKBH8 plays a crucial role in the DNA damage survival pathway through a distinct mechanism involving the regulation of tRNA modification. ALKBH8 localizes to the cytoplasm. It contains the characteristic AlkB domain that is composed of a tRNA methyltransferase motif, a motif homologous to the bacterial AlkB DNA/RNA repair enzyme, and a dioxygenase catalytic core domain encompassing cofactor-binding sites for iron and 2-oxoglutarate. In addition, unlike other AlkB homologs, ALKBH8 contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal S-adenosylmethionine (SAM)-dependent methyltransferase (MT) domain.


Pssm-ID: 409865 [Multi-domain]  Cd Length: 80  Bit Score: 39.49  E-value: 8.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  969 SNIVHISN--LVRPFTLGQLKELLGRTGTlveeafwIDKI-----KSHCFVTYSTVEEAVATRTALHG--VKWPQSNPKF 1039
Cdd:cd12431      1 TQHLVVANggLGNGVSREQLLEVFEKYGT-------VEDIvmlpgKPYSFVSFKSVEEAAKAYNALNGkeLELPQQNVPL 73

                   ....*...
gi 1720380201 1040 LCAdYAEQ 1047
Cdd:cd12431     74 YLS-FVEK 80
PTZ00121 PTZ00121
MAEBL; Provisional
76-402 2.57e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201   76 RVTDLKAALEQRGLAKSGQKSALVKRlkgalMLENLQKHSTPHAAFQPNSQIGEEMSQNSFIKQYLE---KQQELLRQRL 152
Cdd:PTZ00121  1432 KADEAKKKAEEAKKADEAKKKAEEAK-----KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEeakKKADEAKKAA 1506
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  153 E--REAREAAELEGKSSS----FSEEKGESDDEKPRKGERRSSRVRQAKSKLPEYSQTAEEEEDQETPSRNLRVRADRNL 226
Cdd:PTZ00121  1507 EakKKADEAKKAEEAKKAdeakKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  227 KIEEEEEEEEEEEDDDDEEEEEVDEAQKSREA--EAPTLKQFEDE----------EGEERTRAKPEKVVDEKPLNIRSQE 294
Cdd:PTZ00121  1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkiKAEELKKAEEEkkkveqlkkkEAEEKKKAEELKKAEEENKIKAAEE 1666
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  295 KGELE----KGGRVTRSQEEARRSHLARQQQEKETQIVS--LPQEENEVKSSQSL----EEKSQSPSPPPLPEDLEKApv 364
Cdd:PTZ00121  1667 AKKAEedkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEelKKKEAEEKKKAEELkkaeEENKIKAEEAKKEAEEDKK-- 1744
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1720380201  365 vlQPEQIVSEEETPPPLLTKEASSPPTHIQLQEEMEPV 402
Cdd:PTZ00121  1745 --KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
129-412 2.72e-03

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: 42.03  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  129 EEMSQNSFIKQYLEKQQELLRQRLEREAREA--AELEGKSSSFSEEKG-----ESDDEKPRKGERRSS--RVRQAKSKLp 199
Cdd:pfam17380  294 EKMEQERLRQEKEEKAREVERRRKLEEAEKArqAEMDRQAAIYAEQERmamerERELERIRQEERKREleRIRQEEIAM- 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  200 EYSQTAEEEEDQ-ETPSRNLRVRADRNLKIEEEEEEEEEEEDDDDEEEEEVDEAQKSREAEAPTLKQFEDEEGEERTRAK 278
Cdd:pfam17380  373 EISRMRELERLQmERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVR 452
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  279 PEKVVDEKPLNI-------RSQEKGELEKGGRVTRSQEEARRSHLARQQQEKETQIVSLPQE----ENEVKSSQSL---- 343
Cdd:pfam17380  453 LEEQERQQQVERlrqqeeeRKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKrkllEKEMEERQKAiyee 532
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720380201  344 EEKSQSPSPPPLPEDLEKAPVVLQPEQIVSEEETPPPLLTKEASSPPTHIQLQEEMEPVEGPAPPVLIQ 412
Cdd:pfam17380  533 ERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIK 601
RRM_TRMT2A cd12439
RNA recognition motif (RRM) found in tRNA (uracil-5-)-methyltransferase homolog A (TRMT2A) and ...
972-1032 3.44e-03

RNA recognition motif (RRM) found in tRNA (uracil-5-)-methyltransferase homolog A (TRMT2A) and similar proteins; This subfamily corresponds to the RRM of TRMT2A, also known as HpaII tiny fragments locus 9c protein (HTF9C), a novel cell cycle regulated protein. It is an independent biologic factor expressed in tumors associated with clinical outcome in HER2 expressing breast cancer. The function of TRMT2A remains unclear although by sequence homology it has a RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), related to RNA methyltransferases.


Pssm-ID: 409873 [Multi-domain]  Cd Length: 79  Bit Score: 37.61  E-value: 3.44e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720380201  972 VHISNLVRPFTLGQLKELLGRTGtlveeaFWIDKIK-----SHCFVTYSTVEEAVATRTALHGVKW 1032
Cdd:cd12439      8 IEIKNLPKYIGFGQLKKFLQKLG------LKPHKIKligrqTFAFVTFRNEEDRDKALKVLNGHKW 67
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
141-326 4.16e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 4.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  141 LEKQQELLRQRLEREAREAAELEGKSSSFSEEKGESDDEKPRKGERRSSRVRQAKSKLPEYSQTAEEEEDQETPSRNLRV 220
Cdd:COG1196    328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  221 RADRNLKIEEEEEEEeeeeddddeEEEEVDEAQKSREAEAPTLKQFEDEEGEERTRAKPEKVVDEKPLNIRSQEKGELEK 300
Cdd:COG1196    408 AEEALLERLERLEEE---------LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
                          170       180
                   ....*....|....*....|....*.
gi 1720380201  301 GGRVTRSQEEARRSHLARQQQEKETQ 326
Cdd:COG1196    479 LAELLEELAEAAARLLLLLEAEADYE 504
PTZ00121 PTZ00121
MAEBL; Provisional
41-365 4.88e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 4.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201   41 KLPKMPEAVGTDPSTSRKMAELEEVTLDGKPLQALRVTDLKAALEQRGLAKSGQKSALVKRLKGALMLENLQKHSTPHAA 120
Cdd:PTZ00121  1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  121 FQPNSQigEEMSQNSFIKQYLEKQQELLRQRLEREAREAAELEGKSSSFSEEKGESDDEKPRKGERRSSRVRQAKSKLPE 200
Cdd:PTZ00121  1567 EEAKKA--EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  201 YSQTAEEEEDQETPSRnlrVRADRNLKIEEEEEEEEEEEDDDDEEEEEVDEAQKSREAE---APTLKQFEDEEgeertRA 277
Cdd:PTZ00121  1645 EKKKAEELKKAEEENK---IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEakkAEELKKKEAEE-----KK 1716
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  278 KPEKVVDEKPLNIRSQEkgELEKggrvtRSQEEARRSHLARQQQEKETQIVSLPQEEnEVKSSQSLEEKSQSPSPPPLPE 357
Cdd:PTZ00121  1717 KAEELKKAEEENKIKAE--EAKK-----EAEEDKKKAEEAKKDEEEKKKIAHLKKEE-EKKAEEIRKEKEAVIEEELDEE 1788

                   ....*...
gi 1720380201  358 DLEKAPVV 365
Cdd:PTZ00121  1789 DEKRRMEV 1796
PTZ00121 PTZ00121
MAEBL; Provisional
112-362 5.92e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 5.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  112 QKHSTPHAAFQPNSQIGEEMSQNSFIKQYLEKQQELLRQRLErEAREAAEL-EGKSSSFSEEKGESDDEKPRKGERRSSR 190
Cdd:PTZ00121  1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAE-DARKAEEArKAEDARKAEEARKAEDAKRVEIARKAED 1162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  191 VRQAksklpEYSQTAEEEEDQETPSRNLRVRADRNLKieeeeeeeeeeEDDDDEEEEEVDEAQKSREAEaptlkqfEDEE 270
Cdd:PTZ00121  1163 ARKA-----EEARKAEDAKKAEAARKAEEVRKAEELR-----------KAEDARKAEAARKAEEERKAE-------EARK 1219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  271 GEERTRAKPEKVVDEKPLNIRSQEKGELEKGGRVTRSQEEARRSHLARQQ------QEKETQIVSLPQEENEVKSSQSLE 344
Cdd:PTZ00121  1220 AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQaaikaeEARKADELKKAEEKKKADEAKKAE 1299
                          250
                   ....*....|....*...
gi 1720380201  345 EKSQSPSPPPLPEDLEKA 362
Cdd:PTZ00121  1300 EKKKADEAKKKAEEAKKA 1317
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
86-376 8.91e-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: 40.34  E-value: 8.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201   86 QRGLAKSGQKSALVKRLKGALMLENLQKHSTPHAAFQPNSQIGEEMSQNSFIKQYLEKQQELLRQRLEREAREAAELEGK 165
Cdd:pfam02463  665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  166 SSSFSEEKGESDDEKPRKGERRSSRVRQAKSKLPEYSQT--------------AEEEEDQETPSRNLRV--RADRNLKIE 229
Cdd:pfam02463  745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTeklkveeekeeklkAQEEELRALEEELKEEaeLLEEEQLLI 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  230 EEEEEeeeeeddddeeeeeVDEAQKSREAEAPTLKQFEDEEGEERTRAKPEKVVDEKPLNIRSQEKGELEKGGRVTRSQE 309
Cdd:pfam02463  825 EQEEK--------------IKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES 890
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720380201  310 EARRSHLARQQQEKETQIVSLPQEENEVKSSQSLEEKSQSPSPPPLPEDLEKAPVVLQPEQIVSEEE 376
Cdd:pfam02463  891 KEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEE 957
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
373-507 9.17e-03

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 40.24  E-value: 9.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380201  373 SEEETPPPLLTKEASSPPTHIQLQEEMEPVEGPAPPvliQLSPPNT-DAGAREPLASPHPAQLLRSLSPLSGT--TDTKA 449
Cdd:TIGR01348  191 VAGSTPATAPAPASAQPAAQSPAATQPEPAAAPAAA---KAQAPAPqQAGTQNPAKVDHAAPAVRRLAREFGVdlSAVKG 267
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720380201  450 ESPAGRVSDESVLPLAQKSSLPECSTQKGVESEREKSAPLPLTveEFAPAKGITEEPM 507
Cdd:TIGR01348  268 TGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPGALPWPNV--DFSKFGEVEEVDM 323
 
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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