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Conserved domains on  [gi|2462539312|ref|XP_054231589|]
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apoptotic chromatin condensation inducer in the nucleus isoform X5 [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 ...
960-1046 4.36e-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: 165.84  E-value: 4.36e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  960 SNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQD 1039
Cdd:cd12432      1 SRILHIDNLVRPFTLGQLKELLSETGTGVIEGFWMDKIKSHCYVTYSSEEEAVATREALHGVVWPSSNGKRLKVEFVTEE 80

                   ....*..
gi 2462539312 1040 ELDYHRG 1046
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 ...
1155-1185 7.81e-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: 62.44  E-value: 7.81e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462539312 1155 PPAKLLDDLFRKTKAAPCIYWLPLTDSQIVQ 1185
Cdd:pfam16294   50 PPAKLLDDLFRKTKATPCIYWLPLTPEQIAE 80
PTZ00121 super family cl31754
MAEBL; Provisional
141-373 1.69e-07

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.30  E-value: 1.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  141 LEKQQELLRQRLErEAREAAELEGKSSSI--SEEKGDSDDEKPRKGERRSSRVRQARAAKLSEGSQPAEE---EEDQETP 215
Cdd:PTZ00121  1488 AKKKAEEAKKKAD-EAKKAAEAKKKADEAkkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkAEEKKKA 1566
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  216 SRNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKSREAPILKEFKEEGEEMPRVKPEEMMDERPKTRSQEQEVLE 295
Cdd:PTZ00121  1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  296 RGGRFTRSQEEA---RKSHLARQQQEKEMKTTSPLEEEEREIKSSQGLKEKSKSPSppRLTEDRKK-ASLVALPEQTASE 371
Cdd:PTZ00121  1647 KKAEELKKAEEEnkiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK--KAEELKKKeAEEKKKAEELKKA 1724

                   ..
gi 2462539312  372 EE 373
Cdd:PTZ00121  1725 EE 1726
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
72-106 1.62e-06

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


:

Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 45.56  E-value: 1.62e-06
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2462539312    72 LQALRVTDLKAALEQRGLAKSGQKSALVKRLKGAL 106
Cdd:smart00513    1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
 
Name Accession Description Interval E-value
RRM_ACINU cd12432
RNA recognition motif (RRM) found in apoptotic chromatin condensation inducer in the nucleus ...
960-1046 4.36e-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: 165.84  E-value: 4.36e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  960 SNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQD 1039
Cdd:cd12432      1 SRILHIDNLVRPFTLGQLKELLSETGTGVIEGFWMDKIKSHCYVTYSSEEEAVATREALHGVVWPSSNGKRLKVEFVTEE 80

                   ....*..
gi 2462539312 1040 ELDYHRG 1046
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 ...
1155-1185 7.81e-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: 62.44  E-value: 7.81e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462539312 1155 PPAKLLDDLFRKTKAAPCIYWLPLTDSQIVQ 1185
Cdd:pfam16294   50 PPAKLLDDLFRKTKATPCIYWLPLTPEQIAE 80
PTZ00121 PTZ00121
MAEBL; Provisional
141-373 1.69e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.30  E-value: 1.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  141 LEKQQELLRQRLErEAREAAELEGKSSSI--SEEKGDSDDEKPRKGERRSSRVRQARAAKLSEGSQPAEE---EEDQETP 215
Cdd:PTZ00121  1488 AKKKAEEAKKKAD-EAKKAAEAKKKADEAkkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkAEEKKKA 1566
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  216 SRNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKSREAPILKEFKEEGEEMPRVKPEEMMDERPKTRSQEQEVLE 295
Cdd:PTZ00121  1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  296 RGGRFTRSQEEA---RKSHLARQQQEKEMKTTSPLEEEEREIKSSQGLKEKSKSPSppRLTEDRKK-ASLVALPEQTASE 371
Cdd:PTZ00121  1647 KKAEELKKAEEEnkiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK--KAEELKKKeAEEKKKAEELKKA 1724

                   ..
gi 2462539312  372 EE 373
Cdd:PTZ00121  1725 EE 1726
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
72-106 1.62e-06

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


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 45.56  E-value: 1.62e-06
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2462539312    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 4.46e-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: 44.31  E-value: 4.46e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2462539312   72 LQALRVTDLKAALEQRGLAKSGQKSALVKRLKGAL 106
Cdd:pfam02037    1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
129-372 8.16e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.96  E-value: 8.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  129 EEMSQNSFIKQYLEKQQELLRQRLEREAREAAELE-GKSSSISEEKGDSDDEKPRKGER--------RSSRVRQARAAkl 199
Cdd:pfam17380  294 EKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEmDRQAAIYAEQERMAMERERELERirqeerkrELERIRQEEIA-- 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  200 SEGSQPAEEEEDQ-ETPSRNLRVR----ADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKSREAPILKEFKEEGEEMPRV 274
Cdd:pfam17380  372 MEISRMRELERLQmERQQKNERVRqeleAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERV 451
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  275 KPEEMMDERPKTRSQEQEVLERGGRFTRSQEEarkshlaRQQQEKEMKTTSPLEEEEREIKSSQgLKEKSKSPSPPRLTE 354
Cdd:pfam17380  452 RLEEQERQQQVERLRQQEEERKRKKLELEKEK-------RDRKRAEEQRRKILEKELEERKQAM-IEEERKRKLLEKEME 523
                          250
                   ....*....|....*...
gi 2462539312  355 DRKKASLVALPEQTASEE 372
Cdd:pfam17380  524 ERQKAIYEEERRREAEEE 541
 
Name Accession Description Interval E-value
RRM_ACINU cd12432
RNA recognition motif (RRM) found in apoptotic chromatin condensation inducer in the nucleus ...
960-1046 4.36e-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: 165.84  E-value: 4.36e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  960 SNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQD 1039
Cdd:cd12432      1 SRILHIDNLVRPFTLGQLKELLSETGTGVIEGFWMDKIKSHCYVTYSSEEEAVATREALHGVVWPSSNGKRLKVEFVTEE 80

                   ....*..
gi 2462539312 1040 ELDYHRG 1046
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 ...
1155-1185 7.81e-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: 62.44  E-value: 7.81e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462539312 1155 PPAKLLDDLFRKTKAAPCIYWLPLTDSQIVQ 1185
Cdd:pfam16294   50 PPAKLLDDLFRKTKATPCIYWLPLTPEQIAE 80
PTZ00121 PTZ00121
MAEBL; Provisional
141-373 1.69e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.30  E-value: 1.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  141 LEKQQELLRQRLErEAREAAELEGKSSSI--SEEKGDSDDEKPRKGERRSSRVRQARAAKLSEGSQPAEE---EEDQETP 215
Cdd:PTZ00121  1488 AKKKAEEAKKKAD-EAKKAAEAKKKADEAkkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkAEEKKKA 1566
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  216 SRNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKSREAPILKEFKEEGEEMPRVKPEEMMDERPKTRSQEQEVLE 295
Cdd:PTZ00121  1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  296 RGGRFTRSQEEA---RKSHLARQQQEKEMKTTSPLEEEEREIKSSQGLKEKSKSPSppRLTEDRKK-ASLVALPEQTASE 371
Cdd:PTZ00121  1647 KKAEELKKAEEEnkiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK--KAEELKKKeAEEKKKAEELKKA 1724

                   ..
gi 2462539312  372 EE 373
Cdd:PTZ00121  1725 EE 1726
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
72-106 1.62e-06

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


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 45.56  E-value: 1.62e-06
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2462539312    72 LQALRVTDLKAALEQRGLAKSGQKSALVKRLKGAL 106
Cdd:smart00513    1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
PTZ00121 PTZ00121
MAEBL; Provisional
142-372 3.95e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 3.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  142 EKQQELLRQRLEREAREAAELEGKSSSISEEKGDSDDEKPRKGERRSSRVRQARAAKLSEGSQPAE----EEEDQETPSR 217
Cdd:PTZ00121  1531 EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmklYEEEKKMKAE 1610
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  218 NLRVRADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKSREapilkEFKEEgEEMPRVKPEEMM----DERPKT---RSQE 290
Cdd:PTZ00121  1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE-----ELKKA-EEENKIKAAEEAkkaeEDKKKAeeaKKAE 1684
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  291 QEVLERGGRFTRSQEEARKSHLARQQQEKEMKTTSPL--EEEEREIKSSQGLK----EKSKSPSPPRLTEDRKKASLVAL 364
Cdd:PTZ00121  1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELkkAEEENKIKAEEAKKeaeeDKKKAEEAKKDEEEKKKIAHLKK 1764

                   ....*...
gi 2462539312  365 PEQTASEE 372
Cdd:PTZ00121  1765 EEEKKAEE 1772
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
72-106 4.46e-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: 44.31  E-value: 4.46e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2462539312   72 LQALRVTDLKAALEQRGLAKSGQKSALVKRLKGAL 106
Cdd:pfam02037    1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
PTZ00121 PTZ00121
MAEBL; Provisional
142-399 9.02e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 9.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  142 EKQQELLRQRLEREAREAAELEGKSSSIseEKGDSDDEKPRKGERRSSRVRQARAAK--LSEGSQPAEEE---EDQETPS 216
Cdd:PTZ00121  1363 EEKAEAAEKKKEEAKKKADAAKKKAEEK--KKADEAKKKAEEDKKKADELKKAAAAKkkADEAKKKAEEKkkaDEAKKKA 1440
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  217 RNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKSREAPILKEFKEEGEEMPRVKPEEMMDERPKTRSQEQEVLE- 295
Cdd:PTZ00121  1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEe 1520
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  296 -RGGRFTRSQEEARKSHLARQQQEK----EMKTTSPLEEEEREIKSSQGLKEKSKSPSPPRLTEDRKKASLVALPEQTAS 370
Cdd:PTZ00121  1521 aKKADEAKKAEEAKKADEAKKAEEKkkadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
                          250       260       270
                   ....*....|....*....|....*....|..
gi 2462539312  371 EEETPPP---LLTKEASSPPPHPQLHSEEEIE 399
Cdd:PTZ00121  1601 YEEEKKMkaeEAKKAEEAKIKAEELKKAEEEK 1632
PTZ00121 PTZ00121
MAEBL; Provisional
142-397 5.76e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 5.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  142 EKQQELLRQRLErEAREAAELEGKSssisEEKGDSDD-----EKPRKGERRSSRVRQARAAKlsEGSQPAEEEEDQEtps 216
Cdd:PTZ00121  1417 KKKADEAKKKAE-EKKKADEAKKKA----EEAKKADEakkkaEEAKKAEEAKKKAEEAKKAD--EAKKKAEEAKKAD--- 1486
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  217 rNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKSREAPILKEfKEEGEEMPRVKPEEMMDERPKTRSQEQEVLER 296
Cdd:PTZ00121  1487 -EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE-AKKADEAKKAEEKKKADELKKAEELKKAEEKK 1564
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  297 GGRFTRSQEE-----ARKSHLARQQQEKEMKTTSPLEEEEREIKSSQGLKEKskspspprltEDRKKASLVALPEQtasE 371
Cdd:PTZ00121  1565 KAEEAKKAEEdknmaLRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE----------EAKIKAEELKKAEE---E 1631
                          250       260
                   ....*....|....*....|....*.
gi 2462539312  372 EETPPPLLTKEASSPPPHPQLHSEEE 397
Cdd:PTZ00121  1632 KKKVEQLKKKEAEEKKKAEELKKAEE 1657
PTZ00121 PTZ00121
MAEBL; Provisional
142-381 9.56e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 9.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  142 EKQQELLRQRLErEAREAAELEGKSSSISEEKGDSDDEKPRKGERRSSRVRQA--RAAKLSEGSQPAEE----EEDQETP 215
Cdd:PTZ00121  1328 KKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKadAAKKKAEEKKKADEakkkAEEDKKK 1406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  216 SRNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKSREAPILKEFKEEGEEMPRVKPEEMMDERPKTRSQE----- 290
Cdd:PTZ00121  1407 ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakkad 1486
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  291 ------QEVLERGGRFTRSQEEARKSHLARQQQEKEMKTTSPLEEEEREIKSSQGLKEKSKSpSPPRLTEDRKKASLVAL 364
Cdd:PTZ00121  1487 eakkkaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA-DELKKAEELKKAEEKKK 1565
                          250
                   ....*....|....*..
gi 2462539312  365 PEQTASEEETPPPLLTK 381
Cdd:PTZ00121  1566 AEEAKKAEEDKNMALRK 1582
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
75-210 1.27e-04

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 46.37  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312   75 LRVTDLKAALEQRGLAKSGQKSALVKRLKGALMLENLQKHSTPHAAFQPNSQIGE-EMSQNSFIKQYLEKQQELLRQRLE 153
Cdd:PLN03124     5 LKVDELRAALAKRGLDTTGLKAALVRRLDDAIAEDAKTASKSGTKSSAGRKKRRErQDDGDDEPVSPKRIAIDEVKGMTV 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462539312  154 REAREAAELEGKSSSISE----EKGDSDDEKPRKgerRSSRVRQARAAKLSEGSQPAEEEE 210
Cdd:PLN03124    85 RELREAASERGLATTGRKkdllERLCAALESDVK---VGSANGTGEDEKEKGGDEEREKEE 142
PTZ00121 PTZ00121
MAEBL; Provisional
112-384 2.15e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  112 QKHSTPHAAFQPNSQIGEEMSQNSFIKQYLEKQQELLRQRLErEAREAAEL-EGKSSSISEEKGDSDDEKPRKGERRSSR 190
Cdd:PTZ00121  1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAE-DARKAEEArKAEDARKAEEARKAEDAKRVEIARKAED 1162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  191 VRQARAAKLSEGSQPAEEEEDQETPSRNLRVRADRNLKTEEEEEEEeEEEEDDEEEEGDDEGQKSREAPILKEFKEEGEE 270
Cdd:PTZ00121  1163 ARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKA-EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  271 MPRVKPEEMMDERPKTRSQEQEVLERGGRFTRSqEEARKSHLARQQQEK----------EMKTTSPLEEEEREIKSSQGL 340
Cdd:PTZ00121  1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKA-EEARKADELKKAEEKkkadeakkaeEKKKADEAKKKAEEAKKADEA 1320
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2462539312  341 KEKS-----KSPSPPRLTEDRKKASLVALPEQTASEEETPPPLLTKEAS 384
Cdd:PTZ00121  1321 KKKAeeakkKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
PTZ00121 PTZ00121
MAEBL; Provisional
143-401 2.54e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 2.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  143 KQQELLRQRLEREAREAAELEGKSssisEEKGDSDDEKPRKGERRSSRVRQARAAKLSEGSQPAEEEEDQETpsrnLRVR 222
Cdd:PTZ00121  1315 KKADEAKKKAEEAKKKADAAKKKA----EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA----AKKK 1386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  223 ADRNLKTEE-EEEEEEEEEEDDEEEEGDDEGQKSREAPILKEFKEEGEEMPRVKPEEMMDERPKTRSQEQEVLE------ 295
Cdd:PTZ00121  1387 AEEKKKADEaKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEeakkka 1466
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  296 ----RGGRFTRSQEEARKSHLARQQQEKEMKTTSPLEEEEREIKSSQGLK--EKSKSPSPPRLTEDRKKASLVALPEQTA 369
Cdd:PTZ00121  1467 eeakKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKkaEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
                          250       260       270
                   ....*....|....*....|....*....|..
gi 2462539312  370 SEEETPPPLLTKEASSPPPHPQLHSEEEIEPM 401
Cdd:PTZ00121  1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
963-1022 3.77e-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: 3.77e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462539312  963 VHISNLVRPFTLGQLKELLGRTGTlVEEAFWID----KIKSHCFVTYSTVEEAVATRTALHGVK 1022
Cdd:cd00590      1 LFVGNLPPDTTEEDLRELFSKFGE-VVSVRIVRdrdgKSKGFAFVEFESPEDAEKALEALNGTE 63
RRM_ALKBH8 cd12431
RNA recognition motif (RRM) found in alkylated DNA repair protein alkB homolog 8 (ALKBH8) and ...
960-1038 8.01e-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: 8.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  960 SNIVHISN--LVRPFTLGQLKELLGRTGTlveeafwIDKI-----KSHCFVTYSTVEEAVATRTALHG--VKWPQSNPKF 1030
Cdd:cd12431      1 TQHLVVANggLGNGVSREQLLEVFEKYGT-------VEDIvmlpgKPYSFVSFKSVEEAAKAYNALNGkeLELPQQNVPL 73

                   ....*...
gi 2462539312 1031 LCAdYAEQ 1038
Cdd:cd12431     74 YLS-FVEK 80
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
129-372 8.16e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.96  E-value: 8.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  129 EEMSQNSFIKQYLEKQQELLRQRLEREAREAAELE-GKSSSISEEKGDSDDEKPRKGER--------RSSRVRQARAAkl 199
Cdd:pfam17380  294 EKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEmDRQAAIYAEQERMAMERERELERirqeerkrELERIRQEEIA-- 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  200 SEGSQPAEEEEDQ-ETPSRNLRVR----ADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKSREAPILKEFKEEGEEMPRV 274
Cdd:pfam17380  372 MEISRMRELERLQmERQQKNERVRqeleAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERV 451
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  275 KPEEMMDERPKTRSQEQEVLERGGRFTRSQEEarkshlaRQQQEKEMKTTSPLEEEEREIKSSQgLKEKSKSPSPPRLTE 354
Cdd:pfam17380  452 RLEEQERQQQVERLRQQEEERKRKKLELEKEK-------RDRKRAEEQRRKILEKELEERKQAM-IEEERKRKLLEKEME 523
                          250
                   ....*....|....*...
gi 2462539312  355 DRKKASLVALPEQTASEE 372
Cdd:pfam17380  524 ERQKAIYEEERRREAEEE 541
PTZ00121 PTZ00121
MAEBL; Provisional
56-358 1.66e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312   56 SRKMAELEEVTLDGKPLQALRVTDLKAALEQRGlAKSGQKSALVKRLKGALMLENLQKHSTPHAAFQ-----PNSQIGEE 130
Cdd:PTZ00121  1169 ARKAEDAKKAEAARKAEEVRKAEELRKAEDARK-AEAARKAEEERKAEEARKAEDAKKAEAVKKAEEakkdaEEAKKAEE 1247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  131 MSQNSFIKQYLEKQQELLRQRLE----REAREAAEL-------EGKSSSISEEKGDSDDEKPRKGERRSSRVRQARA--- 196
Cdd:PTZ00121  1248 ERNNEEIRKFEEARMAHFARRQAaikaEEARKADELkkaeekkKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAeea 1327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  197 -AKLSEGSQPAEEEEDQETPSRNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKSREAPILKEFKEEGEEMPRVK 275
Cdd:PTZ00121  1328 kKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  276 PEEMMDERPKTRSQE----QEVLERGGRFTRSQEEARKSHLARQQQEKEMKTTSPLEEEEREIKSSQGLK---EKSKSPS 348
Cdd:PTZ00121  1408 DELKKAAAAKKKADEakkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKkaeEAKKADE 1487
                          330
                   ....*....|
gi 2462539312  349 PPRLTEDRKK 358
Cdd:PTZ00121  1488 AKKKAEEAKK 1497
RRM_TRMT2A cd12439
RNA recognition motif (RRM) found in tRNA (uracil-5-)-methyltransferase homolog A (TRMT2A) and ...
963-1023 3.16e-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: 3.16e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462539312  963 VHISNLVRPFTLGQLKELLGRTGtlveeaFWIDKIK-----SHCFVTYSTVEEAVATRTALHGVKW 1023
Cdd:cd12439      8 IEIKNLPKYIGFGQLKKFLQKLG------LKPHKIKligrqTFAFVTFRNEEDRDKALKVLNGHKW 67
PTZ00121 PTZ00121
MAEBL; Provisional
129-362 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 2462539312  129 EEMSQNSFIKQYLEKQQELLRQ-RLEREAREAAElEGKSSSISEEKGDSDDEKPRKGERRSSRVRQARAAKLSEGSQPAE 207
Cdd:PTZ00121  1590 EEARIEEVMKLYEEEKKMKAEEaKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539312  208 EEEDQETPSRNLRvRADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKSREAPILKefKEEGEEMPRVKPEEMMDERPKTR 287
Cdd:PTZ00121  1669 KAEEDKKKAEEAK-KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELK--KAEEENKIKAEEAKKEAEEDKKK 1745
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462539312  288 SQEQEVlerggrftrsqEEARKSHLARQQQEKEMKTTSPLEEEEREIKSSQGLKEKSKSPSPPRLTEDRKKASLV 362
Cdd:PTZ00121  1746 AEEAKK-----------DEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFAN 1809
 
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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