NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034591860|ref|XP_016878065|]
View 

SAFB-like transcription modulator isoform X6 [Homo sapiens]

Protein Classification

RNA-binding protein( domain architecture ID 13917133)

RNA-binding protein recognizes RNA via an RNA recognition motif (RRM); similar to Plasmodium falciparum clustered-asparagine-rich protein (CARP)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RRM_SF super family cl17169
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 367-392 2.01e-11

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).


The actual alignment was detected with superfamily member cd12678:

Pssm-ID: 473069 [Multi-domain]  Cd Length: 74  Bit Score: 60.48  E-value: 2.01e-11
                          10        20
                  ....*....|....*....|....*.
gi 1034591860 367 NIWVSGLSSNTKAADLKNLFGKYGKV 392
Cdd:cd12678     1 NLWVSGLSSNTKAADLKNLFGKYGKV 26
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
22-56 5.05e-08

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


:

Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 49.41  E-value: 5.05e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1034591860   22 ITDLRVIDLKSELKRRNLDITGVKTVLISRLKQAI 56
Cdd:smart00513   1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
PTZ00121 super family cl31754
MAEBL; Provisional
 139-679 3.73e-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: 3.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  139 SKELLSAEENKRAHELIEAEgiediEKEDIESQEIEAQEGEDdtfltaQDGEEEENEKEGSLAEADHTAHEEMEAHTTVK 218
Cdd:PTZ00121  1280 ADELKKAEEKKKADEAKKAE-----EKKKADEAKKKAEEAKK------ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA 1348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  219 EAEDDNISvtiqaedaitldfdgDDLLETGKNVKITDSEASKPKDGQDAIAQSPEKESKDYEMNANHKDGKK--EDCVKG 296
Cdd:PTZ00121  1349 KAEAEAAA---------------DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkaDELKKA 1413

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  297 DPVEKEARESSKKAESGDKEKDTLKKGPSSTGASGQAKSSSKESKDSKTSSKDDKGSTSSTSGSSGSSTKniwvsglssn 376
Cdd:PTZ00121  1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK---------- 1483

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  377 tKAADLKNLfGKYGKVKGDPSKK--EMKKENDEKSSSRSSGDKKNTSDRSSKTQASVKKEEKRSSEKSEKKESKDTKKIE 454
Cdd:PTZ00121  1484 -KADEAKKK-AEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  455 GKDE-KNDNGASGQTSESIKKSEEKKRISSKSPGHMVILDQTKgdhcrpsRRGRYEKIHGRSKEKERASLDKKRDKDYRR 533
Cdd:PTZ00121  1562 EKKKaEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE-------KKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  534 KEILPFEKMKEQRLREHLVRFERLRRAMELRRRREIAERERRERERIRIIREREERERLQRERERLEIERQKLERERMER 613
Cdd:PTZ00121  1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034591860  614 ERLERERIRIEQERRKEAERIAREREELRRQQQQLRYEQEKRNSLKRPRDVDHRRDDPYWSENKKL 679
Cdd:PTZ00121  1715 KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 730-965 9.56e-04

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 9.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  730 GQSEGKKARPTARREDPSFERYPKNFSDSRRNEPPPPRNELRESDRREVRGERDERRTVIIHDRPDITHPRHPREAGPNP 809
Cdd:PHA03307   189 PPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTR 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  810 SR-PTSWKSEGSMSTDKRETRVERPERSGREVSGHSVRGAPPGNRSSASGYGSREGDRGVITDRGGGSQ----HYPEERH 884
Cdd:PHA03307   269 IWeASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRgaavSPGPSPS 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  885 vveRHGRDTSGPrkewhgPPSQGPSyhdTRRMGDGRAGAGMITQHSSNASPINRIVQISGNSMPRGSGSgfkPFKGGPPR 964
Cdd:PHA03307   349 ---RSPSPSRPP------PPADPSS---PRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATG---RFPAGRPR 413


                   .
gi 1034591860  965 R 965
Cdd:PHA03307   414 P 414
 
Name Accession Description Interval E-value
RRM_SLTM cd12678
RNA recognition motif (RRM) found in Scaffold attachment factor (SAF)-like transcription ...
 367-392 2.01e-11

RNA recognition motif (RRM) found in Scaffold attachment factor (SAF)-like transcription modulator (SLTM) and similar proteins; This subgroup corresponds to the RRM domain of SLTM, also termed modulator of estrogen-induced transcription, which shares high sequence similarity with scaffold attachment factor B1 (SAFB1). It contains a scaffold attachment factor-box (SAF-box, also known as SAP domain) DNA-binding motif, an RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a region rich in glutamine and arginine residues. To a large extent, SLTM co-localizes with SAFB1 in the nucleus, which suggests that they share similar functions, such as the inhibition of an oestrogen reporter gene. However, rather than mediating a specific inhibitory effect on oestrogen action, SLTM is shown to exert a generalized inhibitory effect on gene expression associated with induction of apoptosis in a wide range of cell lines.


Pssm-ID: 410079 [Multi-domain]  Cd Length: 74  Bit Score: 60.48  E-value: 2.01e-11
                          10        20
                  ....*....|....*....|....*.
gi 1034591860 367 NIWVSGLSSNTKAADLKNLFGKYGKV 392
Cdd:cd12678     1 NLWVSGLSSNTKAADLKNLFGKYGKV 26
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
22-56 5.05e-08

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


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 49.41  E-value: 5.05e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1034591860   22 ITDLRVIDLKSELKRRNLDITGVKTVLISRLKQAI 56
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 ...
 22-56 1.77e-07

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: 48.17  E-value: 1.77e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1034591860  22 ITDLRVIDLKSELKRRNLDITGVKTVLISRLKQAI 56
Cdd:pfam02037   1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
PTZ00121 PTZ00121
MAEBL; Provisional
 139-679 3.73e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 3.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  139 SKELLSAEENKRAHELIEAEgiediEKEDIESQEIEAQEGEDdtfltaQDGEEEENEKEGSLAEADHTAHEEMEAHTTVK 218
Cdd:PTZ00121  1280 ADELKKAEEKKKADEAKKAE-----EKKKADEAKKKAEEAKK------ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA 1348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  219 EAEDDNISvtiqaedaitldfdgDDLLETGKNVKITDSEASKPKDGQDAIAQSPEKESKDYEMNANHKDGKK--EDCVKG 296
Cdd:PTZ00121  1349 KAEAEAAA---------------DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkaDELKKA 1413

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  297 DPVEKEARESSKKAESGDKEKDTLKKGPSSTGASGQAKSSSKESKDSKTSSKDDKGSTSSTSGSSGSSTKniwvsglssn 376
Cdd:PTZ00121  1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK---------- 1483

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  377 tKAADLKNLfGKYGKVKGDPSKK--EMKKENDEKSSSRSSGDKKNTSDRSSKTQASVKKEEKRSSEKSEKKESKDTKKIE 454
Cdd:PTZ00121  1484 -KADEAKKK-AEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  455 GKDE-KNDNGASGQTSESIKKSEEKKRISSKSPGHMVILDQTKgdhcrpsRRGRYEKIHGRSKEKERASLDKKRDKDYRR 533
Cdd:PTZ00121  1562 EKKKaEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE-------KKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  534 KEILPFEKMKEQRLREHLVRFERLRRAMELRRRREIAERERRERERIRIIREREERERLQRERERLEIERQKLERERMER 613
Cdd:PTZ00121  1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034591860  614 ERLERERIRIEQERRKEAERIAREREELRRQQQQLRYEQEKRNSLKRPRDVDHRRDDPYWSENKKL 679
Cdd:PTZ00121  1715 KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
RRM smart00360
RNA recognition motif;
367-393 9.18e-04

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 38.73  E-value: 9.18e-04
                           10        20
                   ....*....|....*....|....*..
gi 1034591860  367 NIWVSGLSSNTKAADLKNLFGKYGKVK 393
Cdd:smart00360   1 TLFVGNLPPDTTEEELRELFSKFGKVE 27
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 730-965 9.56e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 9.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  730 GQSEGKKARPTARREDPSFERYPKNFSDSRRNEPPPPRNELRESDRREVRGERDERRTVIIHDRPDITHPRHPREAGPNP 809
Cdd:PHA03307   189 PPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTR 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  810 SR-PTSWKSEGSMSTDKRETRVERPERSGREVSGHSVRGAPPGNRSSASGYGSREGDRGVITDRGGGSQ----HYPEERH 884
Cdd:PHA03307   269 IWeASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRgaavSPGPSPS 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  885 vveRHGRDTSGPrkewhgPPSQGPSyhdTRRMGDGRAGAGMITQHSSNASPINRIVQISGNSMPRGSGSgfkPFKGGPPR 964
Cdd:PHA03307   349 ---RSPSPSRPP------PPADPSS---PRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATG---RFPAGRPR 413


                   .
gi 1034591860  965 R 965
Cdd:PHA03307   414 P 414
 
Name Accession Description Interval E-value
RRM_SLTM cd12678
RNA recognition motif (RRM) found in Scaffold attachment factor (SAF)-like transcription ...
 367-392 2.01e-11

RNA recognition motif (RRM) found in Scaffold attachment factor (SAF)-like transcription modulator (SLTM) and similar proteins; This subgroup corresponds to the RRM domain of SLTM, also termed modulator of estrogen-induced transcription, which shares high sequence similarity with scaffold attachment factor B1 (SAFB1). It contains a scaffold attachment factor-box (SAF-box, also known as SAP domain) DNA-binding motif, an RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a region rich in glutamine and arginine residues. To a large extent, SLTM co-localizes with SAFB1 in the nucleus, which suggests that they share similar functions, such as the inhibition of an oestrogen reporter gene. However, rather than mediating a specific inhibitory effect on oestrogen action, SLTM is shown to exert a generalized inhibitory effect on gene expression associated with induction of apoptosis in a wide range of cell lines.


Pssm-ID: 410079 [Multi-domain]  Cd Length: 74  Bit Score: 60.48  E-value: 2.01e-11
                          10        20
                  ....*....|....*....|....*.
gi 1034591860 367 NIWVSGLSSNTKAADLKNLFGKYGKV 392
Cdd:cd12678     1 NLWVSGLSSNTKAADLKNLFGKYGKV 26
RRM_SAFB_like cd12417
RNA recognition motif (RRM) found in the scaffold attachment factor (SAFB) family; This ...
 367-394 4.68e-10

RNA recognition motif (RRM) found in the scaffold attachment factor (SAFB) family; This subfamily corresponds to the RRM domain of the SAFB family, including scaffold attachment factor B1 (SAFB1), scaffold attachment factor B2 (SAFB2), SAFB-like transcriptional modulator (SLTM), and similar proteins, which are ubiquitously expressed. SAFB1, SAFB2 and SLTM have been implicated in many diverse cellular processes including cell growth and transformation, stress response, and apoptosis. They share high sequence similarities and all contain a scaffold attachment factor-box (SAF-box, also known as SAP domain) DNA-binding motif, an RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a region rich in glutamine and arginine residues. SAFB1 is a nuclear protein with a distribution similar to that of SLTM, but unlike that of SAFB2, which is also found in the cytoplasm. To a large extent, SAFB1 and SLTM might share similar functions, such as the inhibition of an oestrogen reporter gene. The additional cytoplasmic localization of SAFB2 implies that it could play additional roles in the cytoplasmic compartment which are distinct from the nuclear functions shared with SAFB1 and SLTM.


Pssm-ID: 409851 [Multi-domain]  Cd Length: 74  Bit Score: 56.49  E-value: 4.68e-10
                          10        20
                  ....*....|....*....|....*...
gi 1034591860 367 NIWVSGLSSNTKAADLKNLFGKYGKVKG 394
Cdd:cd12417     1 NLWISGLSDTTKAADLKKIFSKYGKVVS 28
RRM_SAFB1_SAFB2 cd12679
RNA recognition motif (RRM) found in scaffold attachment factor B1 (SAFB1), scaffold ...
 366-394 9.25e-09

RNA recognition motif (RRM) found in scaffold attachment factor B1 (SAFB1), scaffold attachment factor B2 (SAFB2), and similar proteins; This subgroup corresponds to RRM of SAFB1, also termed scaffold attachment factor B (SAF-B), heat-shock protein 27 estrogen response element ERE and TATA-box-binding protein (HET), or heterogeneous nuclear ribonucleoprotein hnRNP A1- associated protein (HAP), a large multi-domain protein with well-described functions in transcriptional repression, RNA splicing and metabolism, and a proposed role in chromatin organization. Based on the numerous functions, SAFB1 has been implicated in many diverse cellular processes including cell growth and transformation, stress response, and apoptosis. SAFB1 specifically binds to AT-rich scaffold or matrix attachment region DNA elements (S/MAR DNA) by using its N-terminal scaffold attachment factor-box (SAF-box, also known as SAP domain), a homeodomain-like DNA binding motif. The central region of SAFB1 is composed of an RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a nuclear localization signal (NLS). The C-terminus of SAFB1 contains Glu/Arg- and Gly-rich regions that might be involved in protein-protein interaction. Additional studies indicate that the C-terminal region contains a potent and transferable transcriptional repression domain. Another family member is SAFB2, a homolog of SAFB1. Both SAFB1 and SAFB2 are ubiquitously coexpressed and share very high sequence similarity, suggesting that they might function in a similar manner. However, unlike SAFB1, exclusively existing in the nucleus, SAFB2 is also present in the cytoplasm. The additional cytoplasmic localization of SAFB2 implies that it could play additional roles in the cytoplasmic compartment which are distinct from the nuclear functions shared with SAFB1.


Pssm-ID: 410080 [Multi-domain]  Cd Length: 76  Bit Score: 52.97  E-value: 9.25e-09
                          10        20
                  ....*....|....*....|....*....
gi 1034591860 366 KNIWVSGLSSNTKAADLKNLFGKYGKVKG 394
Cdd:cd12679     2 RNLWVSGLSSTTRATDLKNLFSKYGKVVG 30
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
22-56 5.05e-08

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


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 49.41  E-value: 5.05e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1034591860   22 ITDLRVIDLKSELKRRNLDITGVKTVLISRLKQAI 56
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 ...
 22-56 1.77e-07

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: 48.17  E-value: 1.77e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1034591860  22 ITDLRVIDLKSELKRRNLDITGVKTVLISRLKQAI 56
Cdd:pfam02037   1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
PTZ00121 PTZ00121
MAEBL; Provisional
 139-679 3.73e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 3.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  139 SKELLSAEENKRAHELIEAEgiediEKEDIESQEIEAQEGEDdtfltaQDGEEEENEKEGSLAEADHTAHEEMEAHTTVK 218
Cdd:PTZ00121  1280 ADELKKAEEKKKADEAKKAE-----EKKKADEAKKKAEEAKK------ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA 1348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  219 EAEDDNISvtiqaedaitldfdgDDLLETGKNVKITDSEASKPKDGQDAIAQSPEKESKDYEMNANHKDGKK--EDCVKG 296
Cdd:PTZ00121  1349 KAEAEAAA---------------DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkaDELKKA 1413

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  297 DPVEKEARESSKKAESGDKEKDTLKKGPSSTGASGQAKSSSKESKDSKTSSKDDKGSTSSTSGSSGSSTKniwvsglssn 376
Cdd:PTZ00121  1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK---------- 1483

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  377 tKAADLKNLfGKYGKVKGDPSKK--EMKKENDEKSSSRSSGDKKNTSDRSSKTQASVKKEEKRSSEKSEKKESKDTKKIE 454
Cdd:PTZ00121  1484 -KADEAKKK-AEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  455 GKDE-KNDNGASGQTSESIKKSEEKKRISSKSPGHMVILDQTKgdhcrpsRRGRYEKIHGRSKEKERASLDKKRDKDYRR 533
Cdd:PTZ00121  1562 EKKKaEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE-------KKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  534 KEILPFEKMKEQRLREHLVRFERLRRAMELRRRREIAERERRERERIRIIREREERERLQRERERLEIERQKLERERMER 613
Cdd:PTZ00121  1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034591860  614 ERLERERIRIEQERRKEAERIAREREELRRQQQQLRYEQEKRNSLKRPRDVDHRRDDPYWSENKKL 679
Cdd:PTZ00121  1715 KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
RRM smart00360
RNA recognition motif;
367-393 9.18e-04

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 38.73  E-value: 9.18e-04
                           10        20
                   ....*....|....*....|....*..
gi 1034591860  367 NIWVSGLSSNTKAADLKNLFGKYGKVK 393
Cdd:smart00360   1 TLFVGNLPPDTTEEELRELFSKFGKVE 27
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 730-965 9.56e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 9.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  730 GQSEGKKARPTARREDPSFERYPKNFSDSRRNEPPPPRNELRESDRREVRGERDERRTVIIHDRPDITHPRHPREAGPNP 809
Cdd:PHA03307   189 PPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTR 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  810 SR-PTSWKSEGSMSTDKRETRVERPERSGREVSGHSVRGAPPGNRSSASGYGSREGDRGVITDRGGGSQ----HYPEERH 884
Cdd:PHA03307   269 IWeASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRgaavSPGPSPS 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  885 vveRHGRDTSGPrkewhgPPSQGPSyhdTRRMGDGRAGAGMITQHSSNASPINRIVQISGNSMPRGSGSgfkPFKGGPPR 964
Cdd:PHA03307   349 ---RSPSPSRPP------PPADPSS---PRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATG---RFPAGRPR 413


                   .
gi 1034591860  965 R 965
Cdd:PHA03307   414 P 414
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 368-393 2.10e-03

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: 37.65  E-value: 2.10e-03
                          10        20
                  ....*....|....*....|....*.
gi 1034591860 368 IWVSGLSSNTKAADLKNLFGKYGKVK 393
Cdd:cd00590     1 LFVGNLPPDTTEEDLRELFSKFGEVV 26
PTZ00121 PTZ00121
MAEBL; Provisional
 140-668 2.12e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  140 KELLSAEENKRAHELIEAEGIEDIEKEDIESQEIEAQEgEDDTFLTAQDGEEEENEKEGSLAEADHTahEEMEAHTTVKE 219
Cdd:PTZ00121  1215 EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE-EIRKFEEARMAHFARRQAAIKAEEARKA--DELKKAEEKKK 1291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  220 AEDDNISVTI--------QAEDAITLD----------FDGDDLLETGKNVKITDSEASKPKDGQDAIAQSPEKESKDYEM 281
Cdd:PTZ00121  1292 ADEAKKAEEKkkadeakkKAEEAKKADeakkkaeeakKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  282 NANHKDGKKEDCVKGDPVEKEARESSKKAESGDKEKDTLKKGPSSTGASGQAKSSSKESKDSKTSSKDDKGSTSSTSGSS 361
Cdd:PTZ00121  1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  362 GSSTKNiwvsglssntKAADLKNLFGKYGKVKGDPSKKEMKKENDEKSSSRSSGDKKNTSDR---SSKTQASVKKEEKRS 438
Cdd:PTZ00121  1452 KAEEAK----------KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKkaaEAKKKADEAKKAEEA 1521

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  439 SEKSEKKESKDTKKIE--GKDEKNDNGASGQTSESIKKSEEKKRISSKSpghmvildqtKGDHCRPSRRGRYEKIhgRSK 516
Cdd:PTZ00121  1522 KKADEAKKAEEAKKADeaKKAEEKKKADELKKAEELKKAEEKKKAEEAK----------KAEEDKNMALRKAEEA--KKA 1589

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034591860  517 EKERASLDKKRDKDYRRKEILPFEKMKEQRLREHLVRFERLRRAMELRRRREIAERERRERERIRIIREREERERLQRER 596
Cdd:PTZ00121  1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034591860  597 ERLEIERQKLERERMERERLERERIRIEQERRKEAERIAR-EREELRRQQQQLRYEQE---KRNSLKRPRDVDHRR 668
Cdd:PTZ00121  1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKkEAEEKKKAEELKKAEEEnkiKAEEAKKEAEEDKKK 1745
RRM2_MSI cd12323
RNA recognition motif 2 (RRM2) found in RNA-binding protein Musashi homologs Musashi-1, ...
 368-393 7.63e-03

RNA recognition motif 2 (RRM2) found in RNA-binding protein Musashi homologs Musashi-1, Musashi-2 and similar proteins; This subfamily corresponds to the RRM2.in Musashi-1 (also termed Msi1), a neural RNA-binding protein putatively expressed in central nervous system (CNS) stem cells and neural progenitor cells, and associated with asymmetric divisions in neural progenitor cells. It is evolutionarily conserved from invertebrates to vertebrates. Musashi-1 is a homolog of Drosophila Musashi and Xenopus laevis nervous system-specific RNP protein-1 (Nrp-1). It has been implicated in the maintenance of the stem-cell state, differentiation, and tumorigenesis. It translationally regulates the expression of a mammalian numb gene by binding to the 3'-untranslated region of mRNA of Numb, encoding a membrane-associated inhibitor of Notch signaling, and further influences neural development. Moreover, Musashi-1 represses translation by interacting with the poly(A)-binding protein and competes for binding of the eukaryotic initiation factor-4G (eIF-4G). Musashi-2 (also termed Msi2) has been identified as a regulator of the hematopoietic stem cell (HSC) compartment and of leukemic stem cells after transplantation of cells with loss and gain of function of the gene. It influences proliferation and differentiation of HSCs and myeloid progenitors, and further modulates normal hematopoiesis and promotes aggressive myeloid leukemia. Both, Musashi-1 and Musashi-2, contain two conserved N-terminal tandem RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), along with other domains of unknown function.


Pssm-ID: 240769 [Multi-domain]  Cd Length: 74  Bit Score: 36.26  E-value: 7.63e-03
                          10        20
                  ....*....|....*....|....*.
gi 1034591860 368 IWVSGLSSNTKAADLKNLFGKYGKVK 393
Cdd:cd12323     2 IFVGGLSANTTEDDVKKYFSQFGKVE 27
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH