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Conserved domains on  [gi|146231985|ref|NP_075679|]
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apoptotic chromatin condensation inducer in the nucleus isoform 2 [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 ...
 1010-1096 1.75e-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: 167.00  E-value: 1.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146231985 1010 SNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQD 1089
Cdd:cd12432     1 SRILHIDNLVRPFTLGQLKELLSETGTGVIEGFWMDKIKSHCYVTYSSEEEAVATREALHGVVWPSSNGKRLKVEFVTEE 80


                  ....*..
gi 146231985 1090 ELDYHRG 1096
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 ...
 1205-1239 6.87e-15

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: 71.30  E-value: 6.87e-15
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 146231985  1205 PPAKLLDDLFRKTKAAPCIYWLPLTESQIVQKEAE 1239
Cdd:pfam16294   50 PPAKLLDDLFRKTKATPCIYWLPLTPEQIAEKEAQ 84
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
72-106 6.77e-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: 6.77e-07
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 146231985     72 LQALRVTDLKAALEQRGLAKSGQKSALVKRLKGAL 106
Cdd:smart00513    1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
PTZ00121 super family cl31754
MAEBL; Provisional
 210-416 1.43e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146231985  210 SEEKGESDDEKPRKGERRSSRVRQAKsklpeysQTAEEEEDqetpsRNLRVRADRNLKIEEEEEEEEEEEDDDDEEEEEV 289
Cdd:PTZ00121 1542 AEEKKKADELKKAEELKKAEEKKKAE-------EAKKAEED-----KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146231985  290 DEAQKSREA--EAPTLKQFEDEEGEERTRAKPEKVVDEKPLNIRSQEKGELEKGGRVTRSQEEARR--SHLARQQQEKET 365
Cdd:PTZ00121 1610 EEAKKAEEAkiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKkaEEAKKAEEDEKK 1689

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 146231985  366 QIVSLPQEENEVKSSQSLEEKsqSPSPPPLPEDLEKAPVV--LQPEQIVSEEE 416
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKK--EAEEKKKAEELKKAEEEnkIKAEEAKKEAE 1740
PDHac_trf_long super family cl36876
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 413-547 9.34e-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: 9.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146231985   413 SEEETPPPLLTKEASSPPTHIQLQEEMEPVEGPAPPvliQLSPPNT-DAGAREPLASPHPAQLLRSLSPLSGT--TDTKA 489
Cdd:TIGR01348  191 VAGSTPATAPAPASAQPAAQSPAATQPEPAAAPAAA---KAQAPAPqQAGTQNPAKVDHAAPAVRRLAREFGVdlSAVKG 267

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 146231985   490 ESPAGRVSDESVLPLAQKSSLPECSTQKGVESEREKSAPLPLTveEFAPAKGITEEPM 547
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 ...
 1010-1096 1.75e-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: 167.00  E-value: 1.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146231985 1010 SNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQD 1089
Cdd:cd12432     1 SRILHIDNLVRPFTLGQLKELLSETGTGVIEGFWMDKIKSHCYVTYSSEEEAVATREALHGVVWPSSNGKRLKVEFVTEE 80


                  ....*..
gi 146231985 1090 ELDYHRG 1096
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 ...
 1205-1239 6.87e-15

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: 71.30  E-value: 6.87e-15
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 146231985  1205 PPAKLLDDLFRKTKAAPCIYWLPLTESQIVQKEAE 1239
Cdd:pfam16294   50 PPAKLLDDLFRKTKATPCIYWLPLTPEQIAEKEAQ 84
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
72-106 6.77e-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: 6.77e-07
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 146231985     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 2.11e-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: 45.47  E-value: 2.11e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 146231985    72 LQALRVTDLKAALEQRGLAKSGQKSALVKRLKGAL 106
Cdd:pfam02037    1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
PTZ00121 PTZ00121
MAEBL; Provisional
 210-416 1.43e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146231985  210 SEEKGESDDEKPRKGERRSSRVRQAKsklpeysQTAEEEEDqetpsRNLRVRADRNLKIEEEEEEEEEEEDDDDEEEEEV 289
Cdd:PTZ00121 1542 AEEKKKADELKKAEELKKAEEKKKAE-------EAKKAEED-----KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146231985  290 DEAQKSREA--EAPTLKQFEDEEGEERTRAKPEKVVDEKPLNIRSQEKGELEKGGRVTRSQEEARR--SHLARQQQEKET 365
Cdd:PTZ00121 1610 EEAKKAEEAkiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKkaEEAKKAEEDEKK 1689

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 146231985  366 QIVSLPQEENEVKSSQSLEEKsqSPSPPPLPEDLEKAPVV--LQPEQIVSEEE 416
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKK--EAEEKKKAEELKKAEEEnkIKAEEAKKEAE 1740
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 413-547 9.34e-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: 9.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146231985   413 SEEETPPPLLTKEASSPPTHIQLQEEMEPVEGPAPPvliQLSPPNT-DAGAREPLASPHPAQLLRSLSPLSGT--TDTKA 489
Cdd:TIGR01348  191 VAGSTPATAPAPASAQPAAQSPAATQPEPAAAPAAA---KAQAPAPqQAGTQNPAKVDHAAPAVRRLAREFGVdlSAVKG 267

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 146231985   490 ESPAGRVSDESVLPLAQKSSLPECSTQKGVESEREKSAPLPLTveEFAPAKGITEEPM 547
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 ...
 1010-1096 1.75e-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: 167.00  E-value: 1.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146231985 1010 SNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQD 1089
Cdd:cd12432     1 SRILHIDNLVRPFTLGQLKELLSETGTGVIEGFWMDKIKSHCYVTYSSEEEAVATREALHGVVWPSSNGKRLKVEFVTEE 80


                  ....*..
gi 146231985 1090 ELDYHRG 1096
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 ...
 1205-1239 6.87e-15

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: 71.30  E-value: 6.87e-15
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 146231985  1205 PPAKLLDDLFRKTKAAPCIYWLPLTESQIVQKEAE 1239
Cdd:pfam16294   50 PPAKLLDDLFRKTKATPCIYWLPLTPEQIAEKEAQ 84
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
72-106 6.77e-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: 6.77e-07
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 146231985     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 2.11e-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: 45.47  E-value: 2.11e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 146231985    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 ...
 1013-1072 3.91e-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: 3.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 146231985 1013 VHISNLVRPFTLGQLKELLGRTGTlVEEAFWID----KIKSHCFVTYSTVEEAVATRTALHGVK 1072
Cdd:cd00590     1 LFVGNLPPDTTEEDLRELFSKFGE-VVSVRIVRdrdgKSKGFAFVEFESPEDAEKALEALNGTE 63
RRM_ALKBH8 cd12431
RNA recognition motif (RRM) found in alkylated DNA repair protein alkB homolog 8 (ALKBH8) and ...
 1010-1088 8.31e-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: 8.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146231985 1010 SNIVHISN--LVRPFTLGQLKELLGRTGTlveeafwIDKI-----KSHCFVTYSTVEEAVATRTALHG--VKWPQSNPKF 1080
Cdd:cd12431     1 TQHLVVANggLGNGVSREQLLEVFEKYGT-------VEDIvmlpgKPYSFVSFKSVEEAAKAYNALNGkeLELPQQNVPL 73


                  ....*...
gi 146231985 1081 LCAdYAEQ 1088
Cdd:cd12431    74 YLS-FVEK 80
PTZ00121 PTZ00121
MAEBL; Provisional
 210-416 1.43e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146231985  210 SEEKGESDDEKPRKGERRSSRVRQAKsklpeysQTAEEEEDqetpsRNLRVRADRNLKIEEEEEEEEEEEDDDDEEEEEV 289
Cdd:PTZ00121 1542 AEEKKKADELKKAEELKKAEEKKKAE-------EAKKAEED-----KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146231985  290 DEAQKSREA--EAPTLKQFEDEEGEERTRAKPEKVVDEKPLNIRSQEKGELEKGGRVTRSQEEARR--SHLARQQQEKET 365
Cdd:PTZ00121 1610 EEAKKAEEAkiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKkaEEAKKAEEDEKK 1689

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 146231985  366 QIVSLPQEENEVKSSQSLEEKsqSPSPPPLPEDLEKAPVV--LQPEQIVSEEE 416
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKK--EAEEKKKAEELKKAEEEnkIKAEEAKKEAE 1740
RRM_TRMT2A cd12439
RNA recognition motif (RRM) found in tRNA (uracil-5-)-methyltransferase homolog A (TRMT2A) and ...
 1013-1073 3.13e-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: 37.99  E-value: 3.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 146231985 1013 VHISNLVRPFTLGQLKELLGRTGtlveeaFWIDKIK-----SHCFVTYSTVEEAVATRTALHGVKW 1073
Cdd:cd12439     8 IEIKNLPKYIGFGQLKKFLQKLG------LKPHKIKligrqTFAFVTFRNEEDRDKALKVLNGHKW 67
PTZ00121 PTZ00121
MAEBL; Provisional
 210-401 7.58e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 7.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146231985  210 SEEKGESDdEKPRKGERRSSRVRQAksklpEYSQTAEEEEDQETPSRNLRVRADRNLKIEEEEEEEEEEEDDDDEEEEEV 289
Cdd:PTZ00121 1560 AEEKKKAE-EAKKAEEDKNMALRKA-----EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146231985  290 DEAQ--KSREAEAPTLKQFEDEEGEERTRAKPEKVVDE----KPLNIRSQEKGELEKGGRVTRSQEEARRSHLARQQQEK 363
Cdd:PTZ00121 1634 KVEQlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 146231985  364 ETQIVSLPQEENEVKSSQSLEEKSQSPSPPPLPEDLEK 401
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 413-547 9.34e-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: 9.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146231985   413 SEEETPPPLLTKEASSPPTHIQLQEEMEPVEGPAPPvliQLSPPNT-DAGAREPLASPHPAQLLRSLSPLSGT--TDTKA 489
Cdd:TIGR01348  191 VAGSTPATAPAPASAQPAAQSPAATQPEPAAAPAAA---KAQAPAPqQAGTQNPAKVDHAAPAVRRLAREFGVdlSAVKG 267

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 146231985   490 ESPAGRVSDESVLPLAQKSSLPECSTQKGVESEREKSAPLPLTveEFAPAKGITEEPM 547
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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