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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024485524 227 RSILVSGLPSlGIPEDILLDKLELFFSKTKNGGSEVESREFLDDCGQVVLTFTQDGVAEQLITRGQVQVPIGKTKYKLKI 306
Cdd:cd12545     1 RRILVSNLPI-EEPEERILDKLEIFFGKTRNGGGEVDEREFLDDCGSVVLTFVEDGVAKRLTDKGQFEVPFGKRKYKVKV 79

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024485524 166 ALITFEKAEVAQRVIERKEHVVelshgedpeDLDRCQVRVQAGPVDILLPSALEIGLTRGSRSILVSGLPSLGIPEDILL 245
Cdd:pfam07292   1 ALITFEEEGVAQRILKKKKHPV---------PLEKSCVRVKVSPVTLGHLVKFQVFSGVSKRTVLLSGIPDVLEDEEELQ 71

                          90
                  ....*....|....*....
gi 2024485524 246 DKLELFFSKTKNGGSEVES 264
Cdd:pfam07292  72 DKLEIHFQKPSNGGGEVES 90

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024485524 227 RSILVSGLPSlGIPEDILLDKLELFFSKTKNGGSEVESREFLDDCGQVVLTFTQDGVAEQLITRGQVQVPIGKTKYKLKI 306
Cdd:cd12545     1 RRILVSNLPI-EEPEERILDKLEIFFGKTRNGGGEVDEREFLDDCGSVVLTFVEDGVAKRLTDKGQFEVPFGKRKYKVKV 79

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024485524 166 ALITFEKAEVAQRVIERKEHVVelshgedpeDLDRCQVRVQAGPVDILLPSALEIGLTRGSRSILVSGLPSLGIPEDILL 245
Cdd:pfam07292   1 ALITFEEEGVAQRILKKKKHPV---------PLEKSCVRVKVSPVTLGHLVKFQVFSGVSKRTVLLSGIPDVLEDEEELQ 71

                          90
                  ....*....|....*....
gi 2024485524 246 DKLELFFSKTKNGGSEVES 264
Cdd:pfam07292  72 DKLEIHFQKPSNGGGEVES 90

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024485524  27 ERARQEIEQYKDLCRALDQDNAMLQKDKEAVEQRLQHVKKERELLQKNLKQKppKDEKVSLQVDISIAQDEKSRLTQEKQ 106
Cdd:COG1196   270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL--EEELAELEEELEELEEELEELEEELE 347

                          90
                  ....*....|...
gi 2024485524 107 MLENKLEEMRKRI 119
Cdd:COG1196   348 EAEEELEEAEAEL 360

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.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 2024485524 157 VRYPLS-GGSALITFEKAEVAQRVIErKEHVVE 188
Cdd:cd12546    38 VTYPTNtKGVAYVTFEEEEVAQNVLE-KEQVLE 69

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024485524 227 RSILVSGLPSlGIPEDILLDKLELFFSKTKNGGSEVESREFLDDCGQVVLTFTQDGVAEQLITRGQVQVPIGKTKYKLKI 306
Cdd:cd12545     1 RRILVSNLPI-EEPEERILDKLEIFFGKTRNGGGEVDEREFLDDCGSVVLTFVEDGVAKRLTDKGQFEVPFGKRKYKVKV 79

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024485524 166 ALITFEKAEVAQRVIERKEHVVelshgedpeDLDRCQVRVQAGPVDILLPSALEIGLTRGSRSILVSGLPSLGIPEDILL 245
Cdd:pfam07292   1 ALITFEEEGVAQRILKKKKHPV---------PLEKSCVRVKVSPVTLGHLVKFQVFSGVSKRTVLLSGIPDVLEDEEELQ 71

                          90
                  ....*....|....*....
gi 2024485524 246 DKLELFFSKTKNGGSEVES 264
Cdd:pfam07292  72 DKLEIHFQKPSNGGGEVES 90

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024485524 227 RSILVSGLPSLgIPEDILLDKLELFFSKTKNGGSEVESREFLDDCGQVVLTFTQDGVAEQLITRGQVQVPIGKTKYKLKI 306
Cdd:cd12544     1 KKINVSNIPDP-LPDERMRDKLELSFSKPSRGGGEVEDVHYDRESGTAVITFLESGVAERIAKKKHYPFVASCGEHRVTV 79

                  ..
gi 2024485524 307 SP 308
Cdd:cd12544    80 SP 81

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).

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2024485524 331 SGIPDVLAEEPMRDALEIHFQKDSRGGGEVDVLGYVPAGRWAVAVFRE 378
Cdd:cd12544     6 SNIPDPLPDERMRDKLELSFSKPSRGGGEVEDVHYDRESGTAVITFLE 53

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.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2024485524 326 RTVLLSGIPDVLAEEPMRDALEIHFQKDSRGGGEV 360
Cdd:cd12546     1 RTIVVSGLPDDLFEGALKDKLEIHFQRRKNGGGDV 35

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024485524  27 ERARQEIEQYKDLCRALDQDNAMLQKDKEAVEQRLQHVKKERELLQKNLKQKppKDEKVSLQVDISIAQDEKSRLTQEKQ 106
Cdd:COG1196   270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL--EEELAELEEELEELEEELEELEEELE 347

                          90
                  ....*....|...
gi 2024485524 107 MLENKLEEMRKRI 119
Cdd:COG1196   348 EAEEELEEAEAEL 360

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.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 2024485524 157 VRYPLS-GGSALITFEKAEVAQRVIErKEHVVE 188
Cdd:cd12546    38 VTYPTNtKGVAYVTFEEEEVAQNVLE-KEQVLE 69

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.

                          10        20        30
                  ....*....|....*....|....*....|
gi 2024485524 157 VRYPLSGGSALITFEKAEVAQRVIERKEHV 186
Cdd:cd12301    35 VEYLGEKGSAVVTFKDHKVAQRVLAQKKHP 64

RNA recognition motif 1 and 2 in poly [ADP-ribose] polymerase 10 (PARP-10) and similar proteins; This subgroup corresponds to the RRM1 and RRM2 of PARP-10, 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 the 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 play a role in nuclear processes including the regulation of chromatin, gene transcription, and nuclear/cytoplasmic transport. It 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).

                          10        20
                  ....*....|....*....|....*.
gi 2024485524 163 GGSALITFEKAEVAQRVIERKEHVVE 188
Cdd:cd12547    39 GDKAFITFEDPSVAERVLARAEHVLN 64