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Conserved domains on  [gi|188219599|ref|NP_004679|]
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N-myc-interactor [Homo sapiens]

Protein Classification

RRM_NMI and NID domain-containing protein( domain architecture ID 11165786)

protein containing domains IFP_35_N, RRM_NMI, and NID

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NID pfam07292
Nmi/IFP 35 domain (NID); This family represents a domain of approximately 90 residues that is ...
203-292 1.25e-45

Nmi/IFP 35 domain (NID); This family represents a domain of approximately 90 residues that is tandemly repeated within interferon-induced 35 kDa protein (IFP 35) and the homologous N-myc-interactor (Nmi). This domain mediates Nmi-Nmi protein interactions and subcellular localization.


:

Pssm-ID: 462137  Cd Length: 90  Bit Score: 149.52  E-value: 1.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219599  203 AVITFVEIGVADKILKKKEYPLYINQTCHRVTVSPYTEIHLKKYQIFSGTSKRTVLLTGMEGIQMDEEIVEDLINIHFQR 282
Cdd:pfam07292   1 ALITFEEEGVAQRILKKKKHPVPLEKSCVRVKVSPVTLGHLVKFQVFSGVSKRTVLLSGIPDVLEDEEELQDKLEIHFQK 80
                          90
                  ....*....|
gi 188219599  283 AKNGGGEVDV 292
Cdd:pfam07292  81 PSNGGGEVES 90
RRM_NMI cd12544
RNA recognition motif in N-myc-interactor (Nmi) and similar proteins; This subgroup ...
157-237 5.26e-41

RNA recognition motif in N-myc-interactor (Nmi) and similar proteins; This subgroup corresponds to the RRM.in Nmi, also termed N-myc and STAT interactor, an interferon inducible protein that interacts with c-Myc, N-Myc, Max and c-Fos, and other transcription factors containing bHLH-ZIP, bHLH or ZIP domains. In addition to binding Myc proteins, Nmi also associates with all the Stat family of transcription factors except Stat2. In response to cytokines (e.g. IL-2 and IFN-gamma) stimulation, Nmi can enhance Stat-mediated transcriptional activity through recruiting the Stat1 and Stat5 transcriptional coactivators, CREB-binding protein (CBP) and p300. Nmi contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


:

Pssm-ID: 409960  Cd Length: 81  Bit Score: 137.16  E-value: 5.26e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219599 157 MKINVTEIPDTLREDQMRDKLELSFSKSRNGGGEVDRVDYDRQSGSAVITFVEIGVADKILKKKEYPLYINQTCHRVTVS 236
Cdd:cd12544    1 KKINVSNIPDPLPDERMRDKLELSFSKPSRGGGEVEDVHYDRESGTAVITFLESGVAERIAKKKHYPFVASCGEHRVTVS 80

                 .
gi 188219599 237 P 237
Cdd:cd12544   81 P 81
NID pfam07292
Nmi/IFP 35 domain (NID); This family represents a domain of approximately 90 residues that is ...
105-192 3.91e-36

Nmi/IFP 35 domain (NID); This family represents a domain of approximately 90 residues that is tandemly repeated within interferon-induced 35 kDa protein (IFP 35) and the homologous N-myc-interactor (Nmi). This domain mediates Nmi-Nmi protein interactions and subcellular localization.


:

Pssm-ID: 462137  Cd Length: 90  Bit Score: 124.87  E-value: 3.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219599  105 ALITFEKEEVAQNVVSMSKHHVQIKDVNLEVTAKPVPLNSGVRFQVYVEVSKMKINVTEIPDTLR-EDQMRDKLELSFSK 183
Cdd:pfam07292   1 ALITFEEEGVAQRILKKKKHPVPLEKSCVRVKVSPVTLGHLVKFQVFSGVSKRTVLLSGIPDVLEdEEELQDKLEIHFQK 80

                  ....*....
gi 188219599  184 SRNGGGEVD 192
Cdd:pfam07292  81 PSNGGGEVE 89
IFP_35_N pfam07334
Interferon-induced 35 kDa protein (IFP 35) N-terminus; This family represents the N-terminus ...
29-104 8.64e-35

Interferon-induced 35 kDa protein (IFP 35) N-terminus; This family represents the N-terminus of interferon-induced 35 kDa protein (IFP 35) (approximately 80 residues long), which contains a leucine zipper motif in an alpha helical configuration. This family also includes N-myc-interactor (Nmi), a homologous interferon-induced protein.


:

Pssm-ID: 284696  Cd Length: 76  Bit Score: 121.20  E-value: 8.64e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188219599   29 LIDEITKKNIQLKKEIQKLETELQEATKEFQIKEDIPETKMKFLSVETPENDSQLSNISCSFQVSSKVPYEIQKGQ 104
Cdd:pfam07334   1 LIYEITKENIQLKEEIQKLEAELQETTREFQIKEDIPETKIKFTSVETPEDDSQFSNISCSFQVSSKIPYELQKGQ 76
 
Name Accession Description Interval E-value
NID pfam07292
Nmi/IFP 35 domain (NID); This family represents a domain of approximately 90 residues that is ...
203-292 1.25e-45

Nmi/IFP 35 domain (NID); This family represents a domain of approximately 90 residues that is tandemly repeated within interferon-induced 35 kDa protein (IFP 35) and the homologous N-myc-interactor (Nmi). This domain mediates Nmi-Nmi protein interactions and subcellular localization.


Pssm-ID: 462137  Cd Length: 90  Bit Score: 149.52  E-value: 1.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219599  203 AVITFVEIGVADKILKKKEYPLYINQTCHRVTVSPYTEIHLKKYQIFSGTSKRTVLLTGMEGIQMDEEIVEDLINIHFQR 282
Cdd:pfam07292   1 ALITFEEEGVAQRILKKKKHPVPLEKSCVRVKVSPVTLGHLVKFQVFSGVSKRTVLLSGIPDVLEDEEELQDKLEIHFQK 80
                          90
                  ....*....|
gi 188219599  283 AKNGGGEVDV 292
Cdd:pfam07292  81 PSNGGGEVES 90
RRM_NMI cd12544
RNA recognition motif in N-myc-interactor (Nmi) and similar proteins; This subgroup ...
157-237 5.26e-41

RNA recognition motif in N-myc-interactor (Nmi) and similar proteins; This subgroup corresponds to the RRM.in Nmi, also termed N-myc and STAT interactor, an interferon inducible protein that interacts with c-Myc, N-Myc, Max and c-Fos, and other transcription factors containing bHLH-ZIP, bHLH or ZIP domains. In addition to binding Myc proteins, Nmi also associates with all the Stat family of transcription factors except Stat2. In response to cytokines (e.g. IL-2 and IFN-gamma) stimulation, Nmi can enhance Stat-mediated transcriptional activity through recruiting the Stat1 and Stat5 transcriptional coactivators, CREB-binding protein (CBP) and p300. Nmi contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409960  Cd Length: 81  Bit Score: 137.16  E-value: 5.26e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219599 157 MKINVTEIPDTLREDQMRDKLELSFSKSRNGGGEVDRVDYDRQSGSAVITFVEIGVADKILKKKEYPLYINQTCHRVTVS 236
Cdd:cd12544    1 KKINVSNIPDPLPDERMRDKLELSFSKPSRGGGEVEDVHYDRESGTAVITFLESGVAERIAKKKHYPFVASCGEHRVTVS 80

                 .
gi 188219599 237 P 237
Cdd:cd12544   81 P 81
NID pfam07292
Nmi/IFP 35 domain (NID); This family represents a domain of approximately 90 residues that is ...
105-192 3.91e-36

Nmi/IFP 35 domain (NID); This family represents a domain of approximately 90 residues that is tandemly repeated within interferon-induced 35 kDa protein (IFP 35) and the homologous N-myc-interactor (Nmi). This domain mediates Nmi-Nmi protein interactions and subcellular localization.


Pssm-ID: 462137  Cd Length: 90  Bit Score: 124.87  E-value: 3.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219599  105 ALITFEKEEVAQNVVSMSKHHVQIKDVNLEVTAKPVPLNSGVRFQVYVEVSKMKINVTEIPDTLR-EDQMRDKLELSFSK 183
Cdd:pfam07292   1 ALITFEEEGVAQRILKKKKHPVPLEKSCVRVKVSPVTLGHLVKFQVFSGVSKRTVLLSGIPDVLEdEEELQDKLEIHFQK 80

                  ....*....
gi 188219599  184 SRNGGGEVD 192
Cdd:pfam07292  81 PSNGGGEVE 89
IFP_35_N pfam07334
Interferon-induced 35 kDa protein (IFP 35) N-terminus; This family represents the N-terminus ...
29-104 8.64e-35

Interferon-induced 35 kDa protein (IFP 35) N-terminus; This family represents the N-terminus of interferon-induced 35 kDa protein (IFP 35) (approximately 80 residues long), which contains a leucine zipper motif in an alpha helical configuration. This family also includes N-myc-interactor (Nmi), a homologous interferon-induced protein.


Pssm-ID: 284696  Cd Length: 76  Bit Score: 121.20  E-value: 8.64e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188219599   29 LIDEITKKNIQLKKEIQKLETELQEATKEFQIKEDIPETKMKFLSVETPENDSQLSNISCSFQVSSKVPYEIQKGQ 104
Cdd:pfam07334   1 LIYEITKENIQLKEEIQKLEAELQETTREFQIKEDIPETKIKFTSVETPEDDSQFSNISCSFQVSSKIPYELQKGQ 76
RRM2_PAR14 cd12543
RNA recognition motif 2 in vertebrate poly [ADP-ribose] polymerase 14 (PARP-14); This subgroup ...
175-238 2.03e-07

RNA recognition motif 2 in vertebrate poly [ADP-ribose] polymerase 14 (PARP-14); This subgroup corresponds to the RRM2 of PARP-14, also termed aggressive lymphoma protein 2, a member of the B aggressive lymphoma (BAL) family of macrodomain-containing PARPs. It is expressed in B lymphocytes and interacts with the IL-4-induced transcription factor Stat6. It plays a fundamental role in the regulation of IL-4-induced B-cell protection against apoptosis after irradiation or growth factor withdrawal. It mediates IL-4 effects on the levels of gene products that regulate cell survival, proliferation, and lymphomagenesis. PARP-14 acts as a transcriptional switch for Stat6-dependent gene activation. In the presence of IL-4, PARP-14 activates transcription by facilitating the binding of Stat6 to the promoter and release of HDACs from the promoter with an IL-4 signal. In contrast, in the absence of a signal, PARP-14 acts as a transcriptional repressor by recruiting HDACs. Absence of PARP-14 protects against Myc-induced developmental block and lymphoma. Thus, PARP-14 may play an important role in Myc-induced oncogenesis. Additional research indicates that PARP-14 is also a binding partner with phosphoglucose isomerase (PGI)/ autocrine motility factor (AMF). It can inhibit PGI/AMF ubiquitination, thus contributing to its stabilization and secretion. PARP-14 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), three tandem macro domains, and C-terminal region with sequence homology to PARP catalytic domain.


Pssm-ID: 409959  Cd Length: 75  Bit Score: 47.63  E-value: 2.03e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188219599 175 DKLELSFSKSRNGGGEVDRVDYDRQSGSAVITFVEIGVADKILKKKeypLYINQtcHRVTVSPY 238
Cdd:cd12543   16 DYLMLYFENPYNGGIEVDGVTVDPEEESAIITFADPKDVQKIIALK---HQFNK--MPFSVLPY 74
RRM1_2_PAR10_like cd12301
RNA recognition motif 1 and 2 in poly [ADP-ribose] polymerase PARP-10, RNA recognition motif 2 ...
77-135 1.56e-03

RNA recognition motif 1 and 2 in poly [ADP-ribose] polymerase PARP-10, RNA recognition motif 2 in PARP-14, RNA recognition motif in N-myc-interactor (Nmi), interferon-induced 35 kDa protein (IFP 35), RNA-binding protein 43 (RBM43) and similar proteins; This subfamily corresponds to the RRM1 and RRM2 of PARP-10, RRM2 of PARP-14, RRM of N-myc-interactor (Nmi), interferon-induced 35 kDa protein (IFP 35) and RNA-binding protein 43 (RBM43). PARP-10 is a novel oncoprotein c-Myc-interacting protein with poly(ADP-ribose) polymerase activity. It is localized to the nuclear and cytoplasmic compartments. In addition to PARP activity, PARP-10 is also involved in the control of cell proliferation by inhibiting c-Myc- and E1A-mediated cotransformation of primary cells. PARP-10 may also play a role in nuclear processes including the regulation of chromatin, gene transcription, and nuclear/cytoplasmic transport. PARP-10 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two overlapping C-terminal domains composed of a glycine-rich region and a region with homology to catalytic domains of PARP enzymes (PARP domain). In addition, PARP-10 contains two ubiquitin-interacting motifs (UIM). PARP-14, also termed aggressive lymphoma protein 2, is a member of the B aggressive lymphoma (BAL) family of macrodomain-containing PARPs. Like PARP-10, PARP-14 also includes two RRMs at the N-terminus. Nmi, also termed N-myc and STAT interactor, is an interferon inducible protein that interacts with c-Myc, N-Myc, Max and c-Fos, and other transcription factors containing bHLH-ZIP, bHLH or ZIP domains. Besides binding Myc proteins, Nmi also associates with all the Stat family of transcription factors except Stat2. In response to cytokine (e.g. IL-2 and IFN-gamma) stimulation, Nmi can enhance Stat-mediated transcriptional activity through recruiting the Stat1 and Stat5 transcriptional coactivators, CREB-binding protein (CBP) and p300. IFP 35 is an interferon-induced leucine zipper protein that can specifically form homodimers. Distinct from known bZIP proteins, IFP 35 lacks a basic domain critical for DNA binding. In addition, IFP 35 may negatively regulate other bZIP transcription factors by protein-protein interaction. For instance, it can form heterodimers with B-ATF, a member of the AP1 transcription factor family. Both Nmi and IFP35 harbor one RRM. RBM43 is a putative RNA-binding protein containing one RRM, but its biological function remains unclear.


Pssm-ID: 409742 [Multi-domain]  Cd Length: 74  Bit Score: 36.55  E-value: 1.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188219599  77 PENDSQLSNISCSFQVS-------SKVPYEIQKGQALITFEKEEVAQNVVSMSKHHVQIKDVNLEV 135
Cdd:cd12301    9 PEAEALDDKLELYFENSrsgggdvEDVEYLGEKGSAVVTFKDHKVAQRVLAQKKHPLNGMQLSVRP 74
 
Name Accession Description Interval E-value
NID pfam07292
Nmi/IFP 35 domain (NID); This family represents a domain of approximately 90 residues that is ...
203-292 1.25e-45

Nmi/IFP 35 domain (NID); This family represents a domain of approximately 90 residues that is tandemly repeated within interferon-induced 35 kDa protein (IFP 35) and the homologous N-myc-interactor (Nmi). This domain mediates Nmi-Nmi protein interactions and subcellular localization.


Pssm-ID: 462137  Cd Length: 90  Bit Score: 149.52  E-value: 1.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219599  203 AVITFVEIGVADKILKKKEYPLYINQTCHRVTVSPYTEIHLKKYQIFSGTSKRTVLLTGMEGIQMDEEIVEDLINIHFQR 282
Cdd:pfam07292   1 ALITFEEEGVAQRILKKKKHPVPLEKSCVRVKVSPVTLGHLVKFQVFSGVSKRTVLLSGIPDVLEDEEELQDKLEIHFQK 80
                          90
                  ....*....|
gi 188219599  283 AKNGGGEVDV 292
Cdd:pfam07292  81 PSNGGGEVES 90
RRM_NMI cd12544
RNA recognition motif in N-myc-interactor (Nmi) and similar proteins; This subgroup ...
157-237 5.26e-41

RNA recognition motif in N-myc-interactor (Nmi) and similar proteins; This subgroup corresponds to the RRM.in Nmi, also termed N-myc and STAT interactor, an interferon inducible protein that interacts with c-Myc, N-Myc, Max and c-Fos, and other transcription factors containing bHLH-ZIP, bHLH or ZIP domains. In addition to binding Myc proteins, Nmi also associates with all the Stat family of transcription factors except Stat2. In response to cytokines (e.g. IL-2 and IFN-gamma) stimulation, Nmi can enhance Stat-mediated transcriptional activity through recruiting the Stat1 and Stat5 transcriptional coactivators, CREB-binding protein (CBP) and p300. Nmi contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409960  Cd Length: 81  Bit Score: 137.16  E-value: 5.26e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219599 157 MKINVTEIPDTLREDQMRDKLELSFSKSRNGGGEVDRVDYDRQSGSAVITFVEIGVADKILKKKEYPLYINQTCHRVTVS 236
Cdd:cd12544    1 KKINVSNIPDPLPDERMRDKLELSFSKPSRGGGEVEDVHYDRESGTAVITFLESGVAERIAKKKHYPFVASCGEHRVTVS 80

                 .
gi 188219599 237 P 237
Cdd:cd12544   81 P 81
NID pfam07292
Nmi/IFP 35 domain (NID); This family represents a domain of approximately 90 residues that is ...
105-192 3.91e-36

Nmi/IFP 35 domain (NID); This family represents a domain of approximately 90 residues that is tandemly repeated within interferon-induced 35 kDa protein (IFP 35) and the homologous N-myc-interactor (Nmi). This domain mediates Nmi-Nmi protein interactions and subcellular localization.


Pssm-ID: 462137  Cd Length: 90  Bit Score: 124.87  E-value: 3.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219599  105 ALITFEKEEVAQNVVSMSKHHVQIKDVNLEVTAKPVPLNSGVRFQVYVEVSKMKINVTEIPDTLR-EDQMRDKLELSFSK 183
Cdd:pfam07292   1 ALITFEEEGVAQRILKKKKHPVPLEKSCVRVKVSPVTLGHLVKFQVFSGVSKRTVLLSGIPDVLEdEEELQDKLEIHFQK 80

                  ....*....
gi 188219599  184 SRNGGGEVD 192
Cdd:pfam07292  81 PSNGGGEVE 89
IFP_35_N pfam07334
Interferon-induced 35 kDa protein (IFP 35) N-terminus; This family represents the N-terminus ...
29-104 8.64e-35

Interferon-induced 35 kDa protein (IFP 35) N-terminus; This family represents the N-terminus of interferon-induced 35 kDa protein (IFP 35) (approximately 80 residues long), which contains a leucine zipper motif in an alpha helical configuration. This family also includes N-myc-interactor (Nmi), a homologous interferon-induced protein.


Pssm-ID: 284696  Cd Length: 76  Bit Score: 121.20  E-value: 8.64e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188219599   29 LIDEITKKNIQLKKEIQKLETELQEATKEFQIKEDIPETKMKFLSVETPENDSQLSNISCSFQVSSKVPYEIQKGQ 104
Cdd:pfam07334   1 LIYEITKENIQLKEEIQKLEAELQETTREFQIKEDIPETKIKFTSVETPEDDSQFSNISCSFQVSSKIPYELQKGQ 76
RRM1_2_PAR10_like cd12301
RNA recognition motif 1 and 2 in poly [ADP-ribose] polymerase PARP-10, RNA recognition motif 2 ...
157-233 1.63e-26

RNA recognition motif 1 and 2 in poly [ADP-ribose] polymerase PARP-10, RNA recognition motif 2 in PARP-14, RNA recognition motif in N-myc-interactor (Nmi), interferon-induced 35 kDa protein (IFP 35), RNA-binding protein 43 (RBM43) and similar proteins; This subfamily corresponds to the RRM1 and RRM2 of PARP-10, RRM2 of PARP-14, RRM of N-myc-interactor (Nmi), interferon-induced 35 kDa protein (IFP 35) and RNA-binding protein 43 (RBM43). PARP-10 is a novel oncoprotein c-Myc-interacting protein with poly(ADP-ribose) polymerase activity. It is localized to the nuclear and cytoplasmic compartments. In addition to PARP activity, PARP-10 is also involved in the control of cell proliferation by inhibiting c-Myc- and E1A-mediated cotransformation of primary cells. PARP-10 may also play a role in nuclear processes including the regulation of chromatin, gene transcription, and nuclear/cytoplasmic transport. PARP-10 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two overlapping C-terminal domains composed of a glycine-rich region and a region with homology to catalytic domains of PARP enzymes (PARP domain). In addition, PARP-10 contains two ubiquitin-interacting motifs (UIM). PARP-14, also termed aggressive lymphoma protein 2, is a member of the B aggressive lymphoma (BAL) family of macrodomain-containing PARPs. Like PARP-10, PARP-14 also includes two RRMs at the N-terminus. Nmi, also termed N-myc and STAT interactor, is an interferon inducible protein that interacts with c-Myc, N-Myc, Max and c-Fos, and other transcription factors containing bHLH-ZIP, bHLH or ZIP domains. Besides binding Myc proteins, Nmi also associates with all the Stat family of transcription factors except Stat2. In response to cytokine (e.g. IL-2 and IFN-gamma) stimulation, Nmi can enhance Stat-mediated transcriptional activity through recruiting the Stat1 and Stat5 transcriptional coactivators, CREB-binding protein (CBP) and p300. IFP 35 is an interferon-induced leucine zipper protein that can specifically form homodimers. Distinct from known bZIP proteins, IFP 35 lacks a basic domain critical for DNA binding. In addition, IFP 35 may negatively regulate other bZIP transcription factors by protein-protein interaction. For instance, it can form heterodimers with B-ATF, a member of the AP1 transcription factor family. Both Nmi and IFP35 harbor one RRM. RBM43 is a putative RNA-binding protein containing one RRM, but its biological function remains unclear.


Pssm-ID: 409742 [Multi-domain]  Cd Length: 74  Bit Score: 99.34  E-value: 1.63e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 188219599 157 MKINVTEIPDTlreDQMRDKLELSFSKSRNGGGEVDRVDYDRQSGSAVITFVEIGVADKILKKKEYPLYINQTCHRV 233
Cdd:cd12301    1 RSVLVTGLPEA---EALDDKLELYFENSRSGGGDVEDVEYLGEKGSAVVTFKDHKVAQRVLAQKKHPLNGMQLSVRP 74
RRM_IN35 cd12545
RNA recognition motif in interferon-induced 35 kDa protein (IFP 35) and similar proteins; This ...
158-235 1.20e-15

RNA recognition motif in interferon-induced 35 kDa protein (IFP 35) and similar proteins; This subgroup corresponds to the RRM in IFP 35, an interferon-induced leucine zipper protein that can specifically form homodimers. Distinct from known bZIP proteins, IFP 35 lacks a basic domain critical for DNA binding. IFP 35 may negatively regulate other bZIP transcription factors by protein-protein interaction. For instance, it can form heterodimers with B-ATF, a member of the AP1 transcription factor family. IFP 35 contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409961  Cd Length: 79  Bit Score: 70.57  E-value: 1.20e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219599 158 KINVTEIPDTLREDQMRDKLELSFSKSRNGGGEVDRVDYDRQSGSAVITFVEIGVADKILKKKEYPLYINQTCHRVTV 235
Cdd:cd12545    2 RILVSNLPIEEPEERILDKLEIFFGKTRNGGGEVDEREFLDDCGSVVLTFVEDGVAKRLTDKGQFEVPFGKRKYKVKV 79
RRM_RBM43 cd12546
RNA recognition motif in vertebrate RNA-binding protein 43 (RBM43); This subgroup corresponds ...
157-220 4.00e-11

RNA recognition motif in vertebrate RNA-binding protein 43 (RBM43); This subgroup corresponds to the RRM of RBM43, a putative RNA-binding protein containing one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). Although its biological function remains unclear, RBM43 shows high sequence homology to poly [ADP-ribose] polymerase 10 (PARP-10), which is a novel oncoprotein c-Myc-interacting protein with poly(ADP-ribose) polymerase activity.


Pssm-ID: 409962 [Multi-domain]  Cd Length: 77  Bit Score: 58.20  E-value: 4.00e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188219599 157 MKINVTEIPDTLREDQMRDKLELSFSKSRNGGGEVDRVDY-DRQSGSAVITFVEIGVADKILKKK 220
Cdd:cd12546    1 RTIVVSGLPDDLFEGALKDKLEIHFQRRKNGGGDVETVTYpTNTKGVAYVTFEEEEVAQNVLEKE 65
RRM2_PAR14 cd12543
RNA recognition motif 2 in vertebrate poly [ADP-ribose] polymerase 14 (PARP-14); This subgroup ...
175-238 2.03e-07

RNA recognition motif 2 in vertebrate poly [ADP-ribose] polymerase 14 (PARP-14); This subgroup corresponds to the RRM2 of PARP-14, also termed aggressive lymphoma protein 2, a member of the B aggressive lymphoma (BAL) family of macrodomain-containing PARPs. It is expressed in B lymphocytes and interacts with the IL-4-induced transcription factor Stat6. It plays a fundamental role in the regulation of IL-4-induced B-cell protection against apoptosis after irradiation or growth factor withdrawal. It mediates IL-4 effects on the levels of gene products that regulate cell survival, proliferation, and lymphomagenesis. PARP-14 acts as a transcriptional switch for Stat6-dependent gene activation. In the presence of IL-4, PARP-14 activates transcription by facilitating the binding of Stat6 to the promoter and release of HDACs from the promoter with an IL-4 signal. In contrast, in the absence of a signal, PARP-14 acts as a transcriptional repressor by recruiting HDACs. Absence of PARP-14 protects against Myc-induced developmental block and lymphoma. Thus, PARP-14 may play an important role in Myc-induced oncogenesis. Additional research indicates that PARP-14 is also a binding partner with phosphoglucose isomerase (PGI)/ autocrine motility factor (AMF). It can inhibit PGI/AMF ubiquitination, thus contributing to its stabilization and secretion. PARP-14 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), three tandem macro domains, and C-terminal region with sequence homology to PARP catalytic domain.


Pssm-ID: 409959  Cd Length: 75  Bit Score: 47.63  E-value: 2.03e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188219599 175 DKLELSFSKSRNGGGEVDRVDYDRQSGSAVITFVEIGVADKILKKKeypLYINQtcHRVTVSPY 238
Cdd:cd12543   16 DYLMLYFENPYNGGIEVDGVTVDPEEESAIITFADPKDVQKIIALK---HQFNK--MPFSVLPY 74
RRM1_PAR14 cd12300
RNA recognition motif 1 in vertebrate poly [ADP-ribose] polymerase 14 (PARP-14); This ...
173-236 3.65e-05

RNA recognition motif 1 in vertebrate poly [ADP-ribose] polymerase 14 (PARP-14); This subfamily corresponds to the RRM1 of PARP-14, also termed aggressive lymphoma protein 2, a member of the B aggressive lymphoma (BAL) family of macrodomain-containing PARPs. It is expressed in B lymphocytes and interacts with the IL-4-induced transcription factor Stat6. It plays a fundamental role in the regulation of IL-4-induced B-cell protection against apoptosis after irradiation or growth factor withdrawal. It mediates IL-4 effects on the levels of gene products that regulate cell survival, proliferation, and lymphomagenesis. PARP-14 acts as a transcriptional switch for Stat6-dependent gene activation. In the presence of IL-4, PARP-14 activates transcription by facilitating the binding of Stat6 to the promoter and release of HDACs from the promoter with an IL-4 signal. In contrast, in the absence of a signal, PARP-14 acts as a transcriptional repressor by recruiting HDACs. Moreover, the absence of PARP-14 protects against Myc-induced developmental block and lymphoma. Thus, PARP-14 may play an important role in Myc-induced oncogenesis. Research indicates that PARP-14 is also a binding partner with phosphoglucose isomerase (PGI)/ autocrine motility factor (AMF). It can inhibit PGI/AMF ubiquitination, thus contributing to its stabilization and secretion. PARP-14 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), three tandem macro domains, and C-terminal region with sequence homology to PARP catalytic domain.


Pssm-ID: 409741  Cd Length: 82  Bit Score: 41.62  E-value: 3.65e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188219599 173 MRDKLELSF-SKSRNGGGEVDRVDYDRQSGSAVITFVEIGVADKILKKKEYPLYINQTCHRVTVS 236
Cdd:cd12300   18 LKNKLEKYFqSKKRSGGGECTVETEGPSPQTARVSFVNEEVRERVLEKKEHEILQGEGTVRLTVK 82
RRM_RBM43 cd12546
RNA recognition motif in vertebrate RNA-binding protein 43 (RBM43); This subgroup corresponds ...
255-307 5.04e-05

RNA recognition motif in vertebrate RNA-binding protein 43 (RBM43); This subgroup corresponds to the RRM of RBM43, a putative RNA-binding protein containing one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). Although its biological function remains unclear, RBM43 shows high sequence homology to poly [ADP-ribose] polymerase 10 (PARP-10), which is a novel oncoprotein c-Myc-interacting protein with poly(ADP-ribose) polymerase activity.


Pssm-ID: 409962 [Multi-domain]  Cd Length: 77  Bit Score: 40.87  E-value: 5.04e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 188219599 255 RTVLLTGMEGiQMDEEIVEDLINIHFQRAKNGGGEVDVVKCSLGQPHIAY--FEE 307
Cdd:cd12546    1 RTIVVSGLPD-DLFEGALKDKLEIHFQRRKNGGGDVETVTYPTNTKGVAYvtFEE 54
RRM_IN35 cd12545
RNA recognition motif in interferon-induced 35 kDa protein (IFP 35) and similar proteins; This ...
255-292 8.40e-04

RNA recognition motif in interferon-induced 35 kDa protein (IFP 35) and similar proteins; This subgroup corresponds to the RRM in IFP 35, an interferon-induced leucine zipper protein that can specifically form homodimers. Distinct from known bZIP proteins, IFP 35 lacks a basic domain critical for DNA binding. IFP 35 may negatively regulate other bZIP transcription factors by protein-protein interaction. For instance, it can form heterodimers with B-ATF, a member of the AP1 transcription factor family. IFP 35 contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409961  Cd Length: 79  Bit Score: 37.44  E-value: 8.40e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 188219599 255 RTVLLTGMEgIQMDEEIVEDLINIHFQRAKNGGGEVDV 292
Cdd:cd12545    1 RRILVSNLP-IEEPEERILDKLEIFFGKTRNGGGEVDE 37
RRM1_2_PAR10_like cd12301
RNA recognition motif 1 and 2 in poly [ADP-ribose] polymerase PARP-10, RNA recognition motif 2 ...
255-307 1.53e-03

RNA recognition motif 1 and 2 in poly [ADP-ribose] polymerase PARP-10, RNA recognition motif 2 in PARP-14, RNA recognition motif in N-myc-interactor (Nmi), interferon-induced 35 kDa protein (IFP 35), RNA-binding protein 43 (RBM43) and similar proteins; This subfamily corresponds to the RRM1 and RRM2 of PARP-10, RRM2 of PARP-14, RRM of N-myc-interactor (Nmi), interferon-induced 35 kDa protein (IFP 35) and RNA-binding protein 43 (RBM43). PARP-10 is a novel oncoprotein c-Myc-interacting protein with poly(ADP-ribose) polymerase activity. It is localized to the nuclear and cytoplasmic compartments. In addition to PARP activity, PARP-10 is also involved in the control of cell proliferation by inhibiting c-Myc- and E1A-mediated cotransformation of primary cells. PARP-10 may also play a role in nuclear processes including the regulation of chromatin, gene transcription, and nuclear/cytoplasmic transport. PARP-10 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two overlapping C-terminal domains composed of a glycine-rich region and a region with homology to catalytic domains of PARP enzymes (PARP domain). In addition, PARP-10 contains two ubiquitin-interacting motifs (UIM). PARP-14, also termed aggressive lymphoma protein 2, is a member of the B aggressive lymphoma (BAL) family of macrodomain-containing PARPs. Like PARP-10, PARP-14 also includes two RRMs at the N-terminus. Nmi, also termed N-myc and STAT interactor, is an interferon inducible protein that interacts with c-Myc, N-Myc, Max and c-Fos, and other transcription factors containing bHLH-ZIP, bHLH or ZIP domains. Besides binding Myc proteins, Nmi also associates with all the Stat family of transcription factors except Stat2. In response to cytokine (e.g. IL-2 and IFN-gamma) stimulation, Nmi can enhance Stat-mediated transcriptional activity through recruiting the Stat1 and Stat5 transcriptional coactivators, CREB-binding protein (CBP) and p300. IFP 35 is an interferon-induced leucine zipper protein that can specifically form homodimers. Distinct from known bZIP proteins, IFP 35 lacks a basic domain critical for DNA binding. In addition, IFP 35 may negatively regulate other bZIP transcription factors by protein-protein interaction. For instance, it can form heterodimers with B-ATF, a member of the AP1 transcription factor family. Both Nmi and IFP35 harbor one RRM. RBM43 is a putative RNA-binding protein containing one RRM, but its biological function remains unclear.


Pssm-ID: 409742 [Multi-domain]  Cd Length: 74  Bit Score: 36.55  E-value: 1.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 188219599 255 RTVLLTGMEgiqmDEEIVEDLINIHFQRAKNGGGEVDVVKcSLGQPHIAY--FEE 307
Cdd:cd12301    1 RSVLVTGLP----EAEALDDKLELYFENSRSGGGDVEDVE-YLGEKGSAVvtFKD 50
RRM1_2_PAR10_like cd12301
RNA recognition motif 1 and 2 in poly [ADP-ribose] polymerase PARP-10, RNA recognition motif 2 ...
77-135 1.56e-03

RNA recognition motif 1 and 2 in poly [ADP-ribose] polymerase PARP-10, RNA recognition motif 2 in PARP-14, RNA recognition motif in N-myc-interactor (Nmi), interferon-induced 35 kDa protein (IFP 35), RNA-binding protein 43 (RBM43) and similar proteins; This subfamily corresponds to the RRM1 and RRM2 of PARP-10, RRM2 of PARP-14, RRM of N-myc-interactor (Nmi), interferon-induced 35 kDa protein (IFP 35) and RNA-binding protein 43 (RBM43). PARP-10 is a novel oncoprotein c-Myc-interacting protein with poly(ADP-ribose) polymerase activity. It is localized to the nuclear and cytoplasmic compartments. In addition to PARP activity, PARP-10 is also involved in the control of cell proliferation by inhibiting c-Myc- and E1A-mediated cotransformation of primary cells. PARP-10 may also play a role in nuclear processes including the regulation of chromatin, gene transcription, and nuclear/cytoplasmic transport. PARP-10 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two overlapping C-terminal domains composed of a glycine-rich region and a region with homology to catalytic domains of PARP enzymes (PARP domain). In addition, PARP-10 contains two ubiquitin-interacting motifs (UIM). PARP-14, also termed aggressive lymphoma protein 2, is a member of the B aggressive lymphoma (BAL) family of macrodomain-containing PARPs. Like PARP-10, PARP-14 also includes two RRMs at the N-terminus. Nmi, also termed N-myc and STAT interactor, is an interferon inducible protein that interacts with c-Myc, N-Myc, Max and c-Fos, and other transcription factors containing bHLH-ZIP, bHLH or ZIP domains. Besides binding Myc proteins, Nmi also associates with all the Stat family of transcription factors except Stat2. In response to cytokine (e.g. IL-2 and IFN-gamma) stimulation, Nmi can enhance Stat-mediated transcriptional activity through recruiting the Stat1 and Stat5 transcriptional coactivators, CREB-binding protein (CBP) and p300. IFP 35 is an interferon-induced leucine zipper protein that can specifically form homodimers. Distinct from known bZIP proteins, IFP 35 lacks a basic domain critical for DNA binding. In addition, IFP 35 may negatively regulate other bZIP transcription factors by protein-protein interaction. For instance, it can form heterodimers with B-ATF, a member of the AP1 transcription factor family. Both Nmi and IFP35 harbor one RRM. RBM43 is a putative RNA-binding protein containing one RRM, but its biological function remains unclear.


Pssm-ID: 409742 [Multi-domain]  Cd Length: 74  Bit Score: 36.55  E-value: 1.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188219599  77 PENDSQLSNISCSFQVS-------SKVPYEIQKGQALITFEKEEVAQNVVSMSKHHVQIKDVNLEV 135
Cdd:cd12301    9 PEAEALDDKLELYFENSrsgggdvEDVEYLGEKGSAVVTFKDHKVAQRVLAQKKHPLNGMQLSVRP 74
 
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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