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Conserved domains on  [gi|530403270|ref|XP_005267473|]
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apoptotic chromatin condensation inducer in the nucleus isoform X2 [Homo sapiens]

Protein Classification

SAP and RRM_ACINU domain-containing protein( domain architecture ID 11271099)

protein containing domains SAP, PTZ00121, 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 ...
 999-1085 3.53e-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: 166.23  E-value: 3.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  999 SNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQD 1078
Cdd:cd12432     1 SRILHIDNLVRPFTLGQLKELLSETGTGVIEGFWMDKIKSHCYVTYSSEEEAVATREALHGVVWPSSNGKRLKVEFVTEE 80


                  ....*..
gi 530403270 1079 ELDYHRG 1085
Cdd:cd12432    81 ELEELIE 87
RSB_motif super family cl24764
RNSP1-SAP18 binding (RSB) motif; The RSB motif on the Acinus protein is the core around which ...
 1194-1224 4.95e-12

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.


The actual alignment was detected with superfamily member pfam16294:

Pssm-ID: 465085  Cd Length: 91  Bit Score: 63.21  E-value: 4.95e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 530403270  1194 PPAKLLDDLFRKTKAAPCIYWLPLTDSQIVQ 1224
Cdd:pfam16294   50 PPAKLLDDLFRKTKATPCIYWLPLTPEQIAE 80
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
72-106 1.46e-06

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


:

Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 45.94  E-value: 1.46e-06
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 530403270     72 LQALRVTDLKAALEQRGLAKSGQKSALVKRLKGAL 106
Cdd:smart00513    1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
PTZ00121 super family cl31754
MAEBL; Provisional
 210-413 5.14e-06

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  210 SEEKGDSDDEKPRKGERRSSRVRQARAAKLSEGSQPAEEEEDQETPSRNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGD 289
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  290 DEGQKSREAPILKEFKEEGEEIPRVKPEEMMDERPKTRSQEQEVLERGGRFTRSQEEA-------RKSHLARQQQEKEMK 362
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAkkaeedkKKAEEAKKAEEDEKK 1689

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530403270  363 TTSPLEEEEREIKSSQGLKEKSKspspprltEDRKKAslvalpEQTASEEE 413
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEA--------EEKKKA------EELKKAEE 1726
 
Name Accession Description Interval E-value
RRM_ACINU cd12432
RNA recognition motif (RRM) found in apoptotic chromatin condensation inducer in the nucleus ...
 999-1085 3.53e-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: 166.23  E-value: 3.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  999 SNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQD 1078
Cdd:cd12432     1 SRILHIDNLVRPFTLGQLKELLSETGTGVIEGFWMDKIKSHCYVTYSSEEEAVATREALHGVVWPSSNGKRLKVEFVTEE 80


                  ....*..
gi 530403270 1079 ELDYHRG 1085
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 ...
 1194-1224 4.95e-12

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: 63.21  E-value: 4.95e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 530403270  1194 PPAKLLDDLFRKTKAAPCIYWLPLTDSQIVQ 1224
Cdd:pfam16294   50 PPAKLLDDLFRKTKATPCIYWLPLTPEQIAE 80
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
72-106 1.46e-06

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


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 45.94  E-value: 1.46e-06
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 530403270     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 4.01e-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: 44.70  E-value: 4.01e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 530403270    72 LQALRVTDLKAALEQRGLAKSGQKSALVKRLKGAL 106
Cdd:pfam02037    1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
PTZ00121 PTZ00121
MAEBL; Provisional
 210-413 5.14e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  210 SEEKGDSDDEKPRKGERRSSRVRQARAAKLSEGSQPAEEEEDQETPSRNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGD 289
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  290 DEGQKSREAPILKEFKEEGEEIPRVKPEEMMDERPKTRSQEQEVLERGGRFTRSQEEA-------RKSHLARQQQEKEMK 362
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAkkaeedkKKAEEAKKAEEDEKK 1689

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530403270  363 TTSPLEEEEREIKSSQGLKEKSKspspprltEDRKKAslvalpEQTASEEE 413
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEA--------EEKKKA------EELKKAEE 1726
 
Name Accession Description Interval E-value
RRM_ACINU cd12432
RNA recognition motif (RRM) found in apoptotic chromatin condensation inducer in the nucleus ...
 999-1085 3.53e-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: 166.23  E-value: 3.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  999 SNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQD 1078
Cdd:cd12432     1 SRILHIDNLVRPFTLGQLKELLSETGTGVIEGFWMDKIKSHCYVTYSSEEEAVATREALHGVVWPSSNGKRLKVEFVTEE 80


                  ....*..
gi 530403270 1079 ELDYHRG 1085
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 ...
 1194-1224 4.95e-12

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: 63.21  E-value: 4.95e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 530403270  1194 PPAKLLDDLFRKTKAAPCIYWLPLTDSQIVQ 1224
Cdd:pfam16294   50 PPAKLLDDLFRKTKATPCIYWLPLTPEQIAE 80
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
72-106 1.46e-06

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


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 45.94  E-value: 1.46e-06
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 530403270     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 4.01e-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: 44.70  E-value: 4.01e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 530403270    72 LQALRVTDLKAALEQRGLAKSGQKSALVKRLKGAL 106
Cdd:pfam02037    1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
PTZ00121 PTZ00121
MAEBL; Provisional
 210-413 5.14e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  210 SEEKGDSDDEKPRKGERRSSRVRQARAAKLSEGSQPAEEEEDQETPSRNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGD 289
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  290 DEGQKSREAPILKEFKEEGEEIPRVKPEEMMDERPKTRSQEQEVLERGGRFTRSQEEA-------RKSHLARQQQEKEMK 362
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAkkaeedkKKAEEAKKAEEDEKK 1689

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530403270  363 TTSPLEEEEREIKSSQGLKEKSKspspprltEDRKKAslvalpEQTASEEE 413
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEA--------EEKKKA------EELKKAEE 1726
PTZ00121 PTZ00121
MAEBL; Provisional
 218-412 7.90e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 7.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  218 DEKPRKGERRSSRVRQARAAKLSEGSQPAEEEE--DQETPSRNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKS 295
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKlyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  296 REAPILKEFKEEG----EEIPRvKPEEMMDERPKTRSQEQEVLERGGRFTRSQEEARKSHLARQQQEKEMKTTSPL--EE 369
Cdd:PTZ00121 1647 KKAEELKKAEEENkikaAEEAK-KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELkkAE 1725

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 530403270  370 EEREIKSSQGLK----EKSKSPSPPRLTEDRKKASLVALPEQTASEE 412
Cdd:PTZ00121 1726 EENKIKAEEAKKeaeeDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
PTZ00121 PTZ00121
MAEBL; Provisional
 210-413 1.30e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  210 SEEKGDSDDEKPRKGERRSSRVRQARAAKLSEGSQPAEEEEDQETPSRNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGD 289
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA 1453

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  290 DEGQKSREAPILKEFKEEGEEIPRVKPEEMMDERPKTRSQEQEvlERGGRFTRSQEEARKSHLARQQQEKEMKTTSPLEE 369
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK--KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 530403270  370 EEREIKSSQGLKEKSKSpSPPRLTEDRKKASLVALPEQTASEEE 413
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKA-DELKKAEELKKAEEKKKAEEAKKAEE 1574
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 1002-1061 3.89e-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: 3.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530403270 1002 VHISNLVRPFTLGQLKELLGRTGTlVEEAFWID----KIKSHCFVTYSTVEEAVATRTALHGVK 1061
Cdd:cd00590     1 LFVGNLPPDTTEEDLRELFSKFGE-VVSVRIVRdrdgKSKGFAFVEFESPEDAEKALEALNGTE 63
PTZ00121 PTZ00121
MAEBL; Provisional
 210-439 5.66e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 5.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  210 SEEKGDSDDEKPRKGE--RRSSRVRQARAAK--LSEGSQPAEEE---EDQETPSRNLRVRADRNLKTEEEEEEEEEEEED 282
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEdkKKADELKKAAAAKkkADEAKKKAEEKkkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  283 DEEEEGDDEGQKSREAPILKEFKEEGEEIPRVKPEEMMDERPKTRSQEQEVLE--RGGRFTRSQEEARKSHLARQQQEK- 359
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeaKKADEAKKAEEAKKADEAKKAEEKk 1546

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  360 ---EMKTTSPLEEEEREIKSSQGLKEKSKSPSPPRLTEDRKKASLVALPEQTASEEETPPPL---LTKEASSPPPHPQLH 433
Cdd:PTZ00121 1547 kadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeeAKKAEEAKIKAEELK 1626


                  ....*.
gi 530403270  434 SEEEIE 439
Cdd:PTZ00121 1627 KAEEEK 1632
RRM_ALKBH8 cd12431
RNA recognition motif (RRM) found in alkylated DNA repair protein alkB homolog 8 (ALKBH8) and ...
 999-1077 8.26e-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: 8.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  999 SNIVHISN--LVRPFTLGQLKELLGRTGTlveeafwIDKI-----KSHCFVTYSTVEEAVATRTALHG--VKWPQSNPKF 1069
Cdd:cd12431     1 TQHLVVANggLGNGVSREQLLEVFEKYGT-------VEDIvmlpgKPYSFVSFKSVEEAAKAYNALNGkeLELPQQNVPL 73


                  ....*...
gi 530403270 1070 LCAdYAEQ 1077
Cdd:cd12431    74 YLS-FVEK 80
PTZ00121 PTZ00121
MAEBL; Provisional
 210-437 2.02e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  210 SEEKGDSDD-----EKPRKGERRSSRVRQARAAKlsEGSQPAEEEEDQEtpsrNLRVRADRNLKTEEEEEEEEEEEEDDE 284
Cdd:PTZ00121 1440 AEEAKKADEakkkaEEAKKAEEAKKKAEEAKKAD--EAKKKAEEAKKAD----EAKKKAEEAKKKADEAKKAAEAKKKAD 1513

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  285 EEEGDDEGQKSREAPILKEfKEEGEEIPRVKPEEMMDERPKTRSQEQEVLERGGRFTRSQEE-----ARKSHLARQQQEK 359
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEE-AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdknmaLRKAEEAKKAEEA 1592

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530403270  360 EMKTTSPLEEEEREIKSSQGLKEKskspspprltEDRKKASLVALPEQtasEEETPPPLLTKEASSPPPHPQLHSEEE 437
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAE----------EAKIKAEELKKAEE---EKKKVEQLKKKEAEEKKKAEELKKAEE 1657
RRM_TRMT2A cd12439
RNA recognition motif (RRM) found in tRNA (uracil-5-)-methyltransferase homolog A (TRMT2A) and ...
 1002-1062 3.02e-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: 3.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530403270 1002 VHISNLVRPFTLGQLKELLGRTGtlveeaFWIDKIK-----SHCFVTYSTVEEAVATRTALHGVKW 1062
Cdd:cd12439     8 IEIKNLPKYIGFGQLKKFLQKLG------LKPHKIKligrqTFAFVTFRNEEDRDKALKVLNGHKW 67
PTZ00121 PTZ00121
MAEBL; Provisional
 210-441 8.25e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  210 SEEKGDSDDEKPRKGERRSSRVRQARAAKLSEGSQPAEEEEDQETpsrnLRVRADRNLKTEE-EEEEEEEEEEDDEEEEG 288
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA----AKKKAEEKKKADEaKKKAEEDKKKADELKKA 1413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  289 DDEGQKSREAPILKEFKEEGEEIPRVKPEEMMDERPKTRSQEQEVLE----------RGGRFTRSQEEARKSHLARQQQE 358
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEeakkkaeeakKADEAKKKAEEAKKADEAKKKAE 1493

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403270  359 KEMKTTSPLEEEEREIKSSQGLK--EKSKSPSPPRLTEDRKKASLVALPEQTASEEETPPPLLTKEASSPPPHPQLHSEE 436
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKkaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573


                  ....*
gi 530403270  437 EIEPM 441
Cdd:PTZ00121 1574 EDKNM 1578
 
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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