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 50760791   274 VVLTFTQDGVAEQLITRGQVQVPIGKTKYKLKISPYMSGDVTNLQLQPSHCTRTVLLSGIPDVLA-EEPMRDALEIHFQK 352
Cdd:pfam07292   1 ALITFEEEGVAQRILKKKKHPVPLEKSCVRVKVSPVTLGHLVKFQVFSGVSKRTVLLSGIPDVLEdEEELQDKLEIHFQK 80

                          90
                  ....*....|
gi 50760791   353 DSRGGGEVDV 362
Cdd:pfam07292  81 PSNGGGEVES 90

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50760791  27 ERARQEIEQYKDLCRALDQDNAMLQKDKEAVEQRLQHVKKERELLQKNLKQKppKDEKVSLQVDISIAQDEKSRLTQEKQ 106
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL--EEELAELEEELEELEEELEELEEELE 347

                        90
                ....*....|...
gi 50760791 107 MLENKLEEMRKRI 119
Cdd:COG1196 348 EAEEELEEAEAEL 360

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 50760791   274 VVLTFTQDGVAEQLITRGQVQVPIGKTKYKLKISPYMSGDVTNLQLQPSHCTRTVLLSGIPDVLA-EEPMRDALEIHFQK 352
Cdd:pfam07292   1 ALITFEEEGVAQRILKKKKHPVPLEKSCVRVKVSPVTLGHLVKFQVFSGVSKRTVLLSGIPDVLEdEEELQDKLEIHFQK 80

                          90
                  ....*....|
gi 50760791   353 DSRGGGEVDV 362
Cdd:pfam07292  81 PSNGGGEVES 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
                ....*....|....*....|....*....|....*....|....*...
gi 50760791 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 50760791 157 VRYPLS-GGSALITFEKAEVAQRVIEmKEHVVE 188
Cdd:cd12546  38 VTYPTNtKGVAYVTFEEEEVAQNVLE-KEQVLE 69

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50760791    30 RQEIEQYKDLCRALDQDNAMLQKDKEAVEQRLQhvKKERELLQKNLKQKPPKDEKVSLQVDISIAQD------EKSRLTQ 103
Cdd:pfam10174 323 KQHIEVLKESLTAKEQRAAILQTEVDALRLRLE--EKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDmldvkeRKINVLQ 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50760791   104 EKqmLENKLEEMRkrilweDPMMMLRTLPERkvvFKGLTTDKENMDklvltplvryplsggSALITFEKA-EVAQRVIEM 182
Cdd:pfam10174 401 KK--IENLQEQLR------DKDKQLAGLKER---VKSLQTDSSNTD---------------TALTTLEEAlSEKERIIER 454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50760791   183 KEHVVELSHGEDPEDLDrcQVRVQAGPVDILLpSALEIGLTRGSRSIL-----VSGLPSLGIPEDILLDKLELFFSKTKN 257
Cdd:pfam10174 455 LKEQREREDRERLEELE--SLKKENKDLKEKV-SALQPELTEKESSLIdlkehASSLASSGLKKDSKLKSLEIAVEQKKE 531

                  ....*..
gi 50760791   258 GGSEVES 264
Cdd:pfam10174 532 ECSKLEN 538

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 50760791   274 VVLTFTQDGVAEQLITRGQVQVPIGKTKYKLKISPYMSGDVTNLQLQPSHCTRTVLLSGIPDVLA-EEPMRDALEIHFQK 352
Cdd:pfam07292   1 ALITFEEEGVAQRILKKKKHPVPLEKSCVRVKVSPVTLGHLVKFQVFSGVSKRTVLLSGIPDVLEdEEELQDKLEIHFQK 80

                          90
                  ....*....|
gi 50760791   353 DSRGGGEVDV 362
Cdd:pfam07292  81 PSNGGGEVES 90

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        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50760791 227 RSILVSGLPslgiPEDILLDKLELFFSKTKNGGSEVESREFLDDCGQVVLTFTQDGVAEQLITRGqvQVPIGKTKYKL 304
Cdd:cd12301   1 RSVLVTGLP----EAEALDDKLELYFENSRSGGGDVEDVEYLGEKGSAVVTFKDHKVAQRVLAQK--KHPLNGMQLSV 72

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        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50760791 227 RSILVSGLPSlGIPEDILLDKLELFFSKTKNGGSEVESREFLDDCGQVVL-TFTQDGVAEQLITRGQV 293
Cdd:cd12546   1 RTIVVSGLPD-DLFEGALKDKLEIHFQRRKNGGGDVETVTYPTNTKGVAYvTFEEEEVAQNVLEKEQV 67

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
                ....*....|....*....|....*....|....*....|....*....|....
gi 50760791 326 RTVLLSGIPDVLAEEPMRDALEIHFQKDSRGGGEVDVLGYVPAGRWAVAVFRED 379
Cdd:cd12545   1 RRILVSNLPIEEPEERILDKLEIFFGKTRNGGGEVDEREFLDDCGSVVLTFVED 54

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        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 50760791 326 RTVLLSGIPDVLAeepMRDALEIHFQKDSRGGGEVDVLGYVPAGRWAVAVFRED 379
Cdd:cd12301   1 RSVLVTGLPEAEA---LDDKLELYFENSRSGGGDVEDVEYLGEKGSAVVTFKDH 51

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 50760791 157 VRYPLS-GGSALITFEKAEVAQRVIEmKEHVVE 188
Cdd:cd12546  38 VTYPTNtKGVAYVTFEEEEVAQNVLE-KEQVLE 69

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50760791  23 EMSPERaRQEIEQYKDLCRALDQDNAMLQKDKEAVEQRLQHVKKERELLQKNLKQKppKDEKVSLQVDISIAQDEKSRLT 102
Cdd:COG4942 143 YLAPAR-REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER--QKLLARLEKELAELAAELAELQ 219

                        90
                ....*....|....*..
gi 50760791 103 QEKQMLENKLEEMRKRI 119
Cdd:COG4942 220 QEAEELEALIARLEAEA 236

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50760791    30 RQEIEQYKDLCRALDQDNAMLQKDKEAVEQRLQhvKKERELLQKNLKQKPPKDEKVSLQVDISIAQD------EKSRLTQ 103
Cdd:pfam10174 323 KQHIEVLKESLTAKEQRAAILQTEVDALRLRLE--EKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDmldvkeRKINVLQ 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50760791   104 EKqmLENKLEEMRkrilweDPMMMLRTLPERkvvFKGLTTDKENMDklvltplvryplsggSALITFEKA-EVAQRVIEM 182
Cdd:pfam10174 401 KK--IENLQEQLR------DKDKQLAGLKER---VKSLQTDSSNTD---------------TALTTLEEAlSEKERIIER 454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50760791   183 KEHVVELSHGEDPEDLDrcQVRVQAGPVDILLpSALEIGLTRGSRSIL-----VSGLPSLGIPEDILLDKLELFFSKTKN 257
Cdd:pfam10174 455 LKEQREREDRERLEELE--SLKKENKDLKEKV-SALQPELTEKESSLIdlkehASSLASSGLKKDSKLKSLEIAVEQKKE 531

                  ....*..
gi 50760791   258 GGSEVES 264
Cdd:pfam10174 532 ECSKLEN 538