NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|257196179|ref|NP_001158070|]
View 

interferon regulatory factor 2-binding protein 2 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
vRING-HC_IRF2BP2 cd16716
variant of RING finger, HC subclass, found in interferon regulatory factor 2 (IRF2)-binding ...
 486-552 5.26e-42

variant of RING finger, HC subclass, found in interferon regulatory factor 2 (IRF2)-binding protein 2 (IRF-2BP2); IRF-2BP2, also known as IRF-2-binding protein 2 or DIF-1, is a nuclear protein that binds to the C-terminal repression domain of IRF-2 and acts as an IRF-2-dependent transcriptional corepressor, both enhancer-activated and basal transcription. IRF-2BP2 also specifically interacts with the C-terminal domain of the nuclear factor of activated T cells NFAT1 transcription factor, and negatively regulates the NFAT1-dependent transactivation of NFAT-responsive promoters. Moreover, IRF2BP2 suppresses the transactivation activity of p53 on both Bax and p21 promoters. It also shows anti-apoptotic activity through the modulation of the death domain in NRIF3. In addition, IRF2BP2 functions as a cofactor of VGLL4 and plays a critical role controlling gene expression in skeletal, cardiac, and smooth muscle cells. It is a muscle-enriched transcription factor required to activate vascular endothelial growth factor-A (VEGF-A) expression. IRF-2BP2 contains an N-terminal C4-type zinc finger and a C-terminal variant C3HC4-type RING-HC finger. The zinc finger is responsible for the homo- and hetero-dimerization between different members of the IRF-2BP2 family. The RING-HC finger interacts with IRF2 and also with nuclear receptor interacting factor 3 (NRIF3).


:

Pssm-ID: 438376  Cd Length: 67  Bit Score: 145.23  E-value: 5.26e-42
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257196179 486 PLCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRQSIKQQGASGEVYCPSGEKCPLVGSNVPWAFMQG 552
Cdd:cd16716    1 PLCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRESIKQQGATGEVYCPSGEKCPLVGSNVPWAFMQG 67
IRF-2BP1_2 pfam11261
Interferon regulatory factor 2-binding protein zinc finger; IRF-2BP1 and IRF-2BP2 are nuclear ...
 12-63 1.01e-31

Interferon regulatory factor 2-binding protein zinc finger; IRF-2BP1 and IRF-2BP2 are nuclear transcriptional repressor proteins and can inhibit both enhancer-activated and basal transcription. They both contain N-terminal zinc finger represented in this family and C-terminal RING finger domains.


:

Pssm-ID: 463250  Cd Length: 52  Bit Score: 116.47  E-value: 1.01e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 257196179   12 RRQSCYLCDLPRMPWAMIWDFTEPVCRGCVNYEGADRVEFVIETARQLKRAH 63
Cdd:pfam11261   1 RRQKCYLCDLPRGPWAMIWDFSEPVCRGCVNYEGADRIELVIDKARQLKRSH 52
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 70-407 6.92e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 6.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179   70 RSPTGAQPAAAKPPPLSAKDLLLQPPPQLG--HAGAEAARAQAMERYPLAPDRAPRlASDFSTRAGAGLPQSAAQQSAPA 147
Cdd:PHA03247 2602 VDDRGDPRGPAPPSPLPPDTHAPDPPPPSPspAANEPDPHPPPTVPPPERPRDDPA-PGRVSRPRRARRLGRAAQASSPP 2680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179  148 NGILVPNGFSKLEEPPELNRQSPNPRRAHAVPPTLVPLVNGSAALGLSGRAAATLAAVSGTPGLGAQPAELGTHKRPASV 227
Cdd:PHA03247 2681 QRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP 2760

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179  228 SSAAAEHEAREPSKEKAQPAHRSPADSLSSAAGASElsaegagkgRAPGEQDWASRPKTVRDTLLALHQHGH-SGPFESK 306
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRE---------SLPSPWDPADPPAAVLAPAAALPPAASpAGPLPPP 2831

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179  307 FKKEPALTAAGRLLGFEANGANGSKAVARTARKRKPSPEPEGEVGP---PKINGETQPWLSTSTEGLKIPITPTssfvSP 383
Cdd:PHA03247 2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAparPPVRRLARPAVSRSTESFALPPDQP----ER 2907

                         330       340
                  ....*....|....*....|....
gi 257196179  384 PPPTASPHSNRTTPPEAAQNGQSP 407
Cdd:PHA03247 2908 PPQPQAPPPPQPQPQPPPPPQPQP 2931
 
Name Accession Description Interval E-value
vRING-HC_IRF2BP2 cd16716
variant of RING finger, HC subclass, found in interferon regulatory factor 2 (IRF2)-binding ...
 486-552 5.26e-42

variant of RING finger, HC subclass, found in interferon regulatory factor 2 (IRF2)-binding protein 2 (IRF-2BP2); IRF-2BP2, also known as IRF-2-binding protein 2 or DIF-1, is a nuclear protein that binds to the C-terminal repression domain of IRF-2 and acts as an IRF-2-dependent transcriptional corepressor, both enhancer-activated and basal transcription. IRF-2BP2 also specifically interacts with the C-terminal domain of the nuclear factor of activated T cells NFAT1 transcription factor, and negatively regulates the NFAT1-dependent transactivation of NFAT-responsive promoters. Moreover, IRF2BP2 suppresses the transactivation activity of p53 on both Bax and p21 promoters. It also shows anti-apoptotic activity through the modulation of the death domain in NRIF3. In addition, IRF2BP2 functions as a cofactor of VGLL4 and plays a critical role controlling gene expression in skeletal, cardiac, and smooth muscle cells. It is a muscle-enriched transcription factor required to activate vascular endothelial growth factor-A (VEGF-A) expression. IRF-2BP2 contains an N-terminal C4-type zinc finger and a C-terminal variant C3HC4-type RING-HC finger. The zinc finger is responsible for the homo- and hetero-dimerization between different members of the IRF-2BP2 family. The RING-HC finger interacts with IRF2 and also with nuclear receptor interacting factor 3 (NRIF3).


Pssm-ID: 438376  Cd Length: 67  Bit Score: 145.23  E-value: 5.26e-42
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257196179 486 PLCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRQSIKQQGASGEVYCPSGEKCPLVGSNVPWAFMQG 552
Cdd:cd16716    1 PLCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRESIKQQGATGEVYCPSGEKCPLVGSNVPWAFMQG 67
IRF-2BP1_2 pfam11261
Interferon regulatory factor 2-binding protein zinc finger; IRF-2BP1 and IRF-2BP2 are nuclear ...
 12-63 1.01e-31

Interferon regulatory factor 2-binding protein zinc finger; IRF-2BP1 and IRF-2BP2 are nuclear transcriptional repressor proteins and can inhibit both enhancer-activated and basal transcription. They both contain N-terminal zinc finger represented in this family and C-terminal RING finger domains.


Pssm-ID: 463250  Cd Length: 52  Bit Score: 116.47  E-value: 1.01e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 257196179   12 RRQSCYLCDLPRMPWAMIWDFTEPVCRGCVNYEGADRVEFVIETARQLKRAH 63
Cdd:pfam11261   1 RRQKCYLCDLPRGPWAMIWDFSEPVCRGCVNYEGADRIELVIDKARQLKRSH 52
PHA03247 PHA03247
large tegument protein UL36; Provisional
 70-407 6.92e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 6.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179   70 RSPTGAQPAAAKPPPLSAKDLLLQPPPQLG--HAGAEAARAQAMERYPLAPDRAPRlASDFSTRAGAGLPQSAAQQSAPA 147
Cdd:PHA03247 2602 VDDRGDPRGPAPPSPLPPDTHAPDPPPPSPspAANEPDPHPPPTVPPPERPRDDPA-PGRVSRPRRARRLGRAAQASSPP 2680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179  148 NGILVPNGFSKLEEPPELNRQSPNPRRAHAVPPTLVPLVNGSAALGLSGRAAATLAAVSGTPGLGAQPAELGTHKRPASV 227
Cdd:PHA03247 2681 QRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP 2760

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179  228 SSAAAEHEAREPSKEKAQPAHRSPADSLSSAAGASElsaegagkgRAPGEQDWASRPKTVRDTLLALHQHGH-SGPFESK 306
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRE---------SLPSPWDPADPPAAVLAPAAALPPAASpAGPLPPP 2831

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179  307 FKKEPALTAAGRLLGFEANGANGSKAVARTARKRKPSPEPEGEVGP---PKINGETQPWLSTSTEGLKIPITPTssfvSP 383
Cdd:PHA03247 2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAparPPVRRLARPAVSRSTESFALPPDQP----ER 2907

                         330       340
                  ....*....|....*....|....
gi 257196179  384 PPPTASPHSNRTTPPEAAQNGQSP 407
Cdd:PHA03247 2908 PPQPQAPPPPQPQPQPPPPPQPQP 2931
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 489-533 9.39e-03

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 34.41  E-value: 9.39e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 257196179   489 CTLCHER-LEDTHFVQCpsvpSHKFCFPCSRQSIKQQGASgevyCP 533
Cdd:smart00184   1 CPICLEEyLKDPVILPC----GHTFCRSCIRKWLESGNNT----CP 38
 
Name Accession Description Interval E-value
vRING-HC_IRF2BP2 cd16716
variant of RING finger, HC subclass, found in interferon regulatory factor 2 (IRF2)-binding ...
 486-552 5.26e-42

variant of RING finger, HC subclass, found in interferon regulatory factor 2 (IRF2)-binding protein 2 (IRF-2BP2); IRF-2BP2, also known as IRF-2-binding protein 2 or DIF-1, is a nuclear protein that binds to the C-terminal repression domain of IRF-2 and acts as an IRF-2-dependent transcriptional corepressor, both enhancer-activated and basal transcription. IRF-2BP2 also specifically interacts with the C-terminal domain of the nuclear factor of activated T cells NFAT1 transcription factor, and negatively regulates the NFAT1-dependent transactivation of NFAT-responsive promoters. Moreover, IRF2BP2 suppresses the transactivation activity of p53 on both Bax and p21 promoters. It also shows anti-apoptotic activity through the modulation of the death domain in NRIF3. In addition, IRF2BP2 functions as a cofactor of VGLL4 and plays a critical role controlling gene expression in skeletal, cardiac, and smooth muscle cells. It is a muscle-enriched transcription factor required to activate vascular endothelial growth factor-A (VEGF-A) expression. IRF-2BP2 contains an N-terminal C4-type zinc finger and a C-terminal variant C3HC4-type RING-HC finger. The zinc finger is responsible for the homo- and hetero-dimerization between different members of the IRF-2BP2 family. The RING-HC finger interacts with IRF2 and also with nuclear receptor interacting factor 3 (NRIF3).


Pssm-ID: 438376  Cd Length: 67  Bit Score: 145.23  E-value: 5.26e-42
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257196179 486 PLCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRQSIKQQGASGEVYCPSGEKCPLVGSNVPWAFMQG 552
Cdd:cd16716    1 PLCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRESIKQQGATGEVYCPSGEKCPLVGSNVPWAFMQG 67
vRING-HC_IRF2BPL cd16717
variant of RING finger, HC subclass, found in interferon regulatory factor 2-binding ...
 482-547 1.43e-38

variant of RING finger, HC subclass, found in interferon regulatory factor 2-binding protein-like (IRF-2BPL); IRF-2BPL, also known as C14orf4 or enhanced at puberty protein 1(EAP1), is a homolog of interferon regulatory factor 2-binding proteins, IRF-2BP1 and IRF-2BP2. It is expressed in the mediobasal hypothalamus and plays a critical function in regulating the female reproductive neuroendocrine axis. IRF-2BPL is a proline-rich protein with polyglutamine and polyalanine tracks at the N-terminus and a C3HC4-type RING-HC finger domain with a partially new pattern at the C-terminus.


Pssm-ID: 438377  Cd Length: 66  Bit Score: 135.61  E-value: 1.43e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257196179 482 AASAPLCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRQSIKQQGASGEVYCPSGEKCPLVGSNVPW 547
Cdd:cd16717    1 ANSGPLCCTICHERLEDTHFVQCPSVPSHKFCFPCSRESIKAQGATGEVYCPSGEKCPLVGSNVPW 66
vRING-HC_IRF2BP1 cd16715
variant of RING finger, HC subclass, found in interferon regulatory factor 2-binding protein 1 ...
 486-547 3.91e-37

variant of RING finger, HC subclass, found in interferon regulatory factor 2-binding protein 1 (IRF-2BP1); IRF-2BP1, also known as IRF-2-binding protein 1, is a nuclear protein that binds to the C-terminal repression domain of IRF-2 and acts as an IRF-2-dependent transcriptional corepressor, both enhancer-activated and basal transcription. It binds to Jun-dimerization protein 2 (JDP2), a member of the activating protein-1 (AP-1) family of transcription factors, and enhances the polyubiquitination of JDP2. It also represses activating transcription factor-2 (ATF2)-mediated transcriptional activation from a cyclic AMP-responsive element (CRE)-containing promoter. IRF-2BP1 contains an N-terminal C4-type zinc finger and a C-terminal variant C3HC4-type RING-HC finger.


Pssm-ID: 438375  Cd Length: 62  Bit Score: 131.65  E-value: 3.91e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257196179 486 PLCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRQSIKQQGASGEVYCPSGEKCPLVGSNVPW 547
Cdd:cd16715    1 PLCCTICHERLEDTHFVQCPSVPGHKFCFPCSRDFIKAQGPAGEVYCPSGDKCPLVGSNVPW 62
vRING-HC_IRF2BP1-like cd16511
variant of RING finger, HC subclass, found in interferon regulatory factor 2-binding protein ...
 487-542 1.71e-36

variant of RING finger, HC subclass, found in interferon regulatory factor 2-binding protein IRF-2BP1, IRF-2BP2, and similar proteins; This subfamily includes IRF-2BP1, IRF-2BP2, and their homolog, IRF-2BP-like, also known as IRF-2BPL or C14orf4. IRF-2BP1 and IRF-2BP2 are nuclear proteins that bind to the C-terminal repression domain of IRF-2 and act as IRF-2-dependent transcriptional corepressors, both enhancer-activated and basal transcription. IRF-2BPL is expressed in the mediobasal hypothalamus and plays a critical function in regulating the female reproductive neuroendocrine axis. All subfamily members contain a C-terminal variant C3HC4-type RING-HC finger.


Pssm-ID: 438174  Cd Length: 56  Bit Score: 129.85  E-value: 1.71e-36
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 257196179 487 LCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRQSIKQQGASGEVYCPSGEKCPLVG 542
Cdd:cd16511    1 LCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRDSIKRQGAGGEVYCPSGEKCPLVG 56
IRF-2BP1_2 pfam11261
Interferon regulatory factor 2-binding protein zinc finger; IRF-2BP1 and IRF-2BP2 are nuclear ...
 12-63 1.01e-31

Interferon regulatory factor 2-binding protein zinc finger; IRF-2BP1 and IRF-2BP2 are nuclear transcriptional repressor proteins and can inhibit both enhancer-activated and basal transcription. They both contain N-terminal zinc finger represented in this family and C-terminal RING finger domains.


Pssm-ID: 463250  Cd Length: 52  Bit Score: 116.47  E-value: 1.01e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 257196179   12 RRQSCYLCDLPRMPWAMIWDFTEPVCRGCVNYEGADRVEFVIETARQLKRAH 63
Cdd:pfam11261   1 RRQKCYLCDLPRGPWAMIWDFSEPVCRGCVNYEGADRIELVIDKARQLKRSH 52
PHA03247 PHA03247
large tegument protein UL36; Provisional
 70-407 6.92e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 6.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179   70 RSPTGAQPAAAKPPPLSAKDLLLQPPPQLG--HAGAEAARAQAMERYPLAPDRAPRlASDFSTRAGAGLPQSAAQQSAPA 147
Cdd:PHA03247 2602 VDDRGDPRGPAPPSPLPPDTHAPDPPPPSPspAANEPDPHPPPTVPPPERPRDDPA-PGRVSRPRRARRLGRAAQASSPP 2680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179  148 NGILVPNGFSKLEEPPELNRQSPNPRRAHAVPPTLVPLVNGSAALGLSGRAAATLAAVSGTPGLGAQPAELGTHKRPASV 227
Cdd:PHA03247 2681 QRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP 2760

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179  228 SSAAAEHEAREPSKEKAQPAHRSPADSLSSAAGASElsaegagkgRAPGEQDWASRPKTVRDTLLALHQHGH-SGPFESK 306
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRE---------SLPSPWDPADPPAAVLAPAAALPPAASpAGPLPPP 2831

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179  307 FKKEPALTAAGRLLGFEANGANGSKAVARTARKRKPSPEPEGEVGP---PKINGETQPWLSTSTEGLKIPITPTssfvSP 383
Cdd:PHA03247 2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAparPPVRRLARPAVSRSTESFALPPDQP----ER 2907

                         330       340
                  ....*....|....*....|....
gi 257196179  384 PPPTASPHSNRTTPPEAAQNGQSP 407
Cdd:PHA03247 2908 PPQPQAPPPPQPQPQPPPPPQPQP 2931
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
 487-533 4.09e-05

HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to the HC subclass of RING (RING-HC) fingers that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC fingers can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438113 [Multi-domain]  Cd Length: 41  Bit Score: 40.93  E-value: 4.09e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 257196179 487 LCCTLCHERLEDTHFVQCpsvpSHKFCFPCSRQSIKqqgaSGEVYCP 533
Cdd:cd16449    1 LECPICLERLKDPVLLPC----GHVFCRECIRRLLE----SGSIKCP 39
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 111-487 2.39e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179  111 MERYPLAPDRAPRLASDFSTRAGAGLPQSAAQQSAPANGILVPNGFSKLEEPPELNRQSPNPRRAHAVPPTLVPlvngsa 190
Cdd:PHA03307   67 PPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRP------ 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179  191 aLGLSGRAAATLAAVSGTPglGAQPAELGTHKRPASVSSAAAEHEAREPSKEKAQPAHRSPADSLSSAAGA--SELSAEG 268
Cdd:PHA03307  141 -VGSPGPPPAASPPAAGAS--PAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRrsSPISASA 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179  269 AGKGRAPGEQDWASRPKTVRDTLLALHQHGHSGPFESKFKKEPALTAAGRLLGfEANGANGSKAVARTARKRKPSPEPEG 348
Cdd:PHA03307  218 SSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIW-EASGWNGPSSRPGPASSSSSPRERSP 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179  349 EVGPPK-INGETQPWLSTSTEGLKIPITPTSSFVSPPPPTASPHSNRTTPPEAAQNGQSPmaalilvADNAGGSHASKDA 427
Cdd:PHA03307  297 SPSPSSpGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRP-------PPPADPSSPRKRP 369

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 257196179  428 TQVHSTTRRNSSSPPSPSSMNQRRLGPREVGGQATGSTGGLEPvhPASLPDSSLAASAPL 487
Cdd:PHA03307  370 RPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRP--RPSPLDAGAASGAFY 427
RING-HC_RBR_HEL2-like cd16625
RING finger, HC subclass, found in Saccharomyces cerevisiae histone E3 ligase 2 (HEL2) and ...
 489-541 8.71e-03

RING finger, HC subclass, found in Saccharomyces cerevisiae histone E3 ligase 2 (HEL2) and similar proteins; HEL2 is an E3 ubiquitin-protein ligase that interacts with the E2 ubiquitin-conjugating enzyme UBC4 and histones H3 and H4. It plays an important role in regulating histone protein levels and also likely to contribute to the maintenance of genomic stability in the budding yeast. HEL2 can be phosphorylated by the DNA damage checkpoint kinase and histone protein regulator Rad53. This subfamily also includes Schizosaccharomyces pombe histone E3 ligase 1 (HEL1), also known as DNA-break-localizing protein 4 (dbl4), and Dictyostelium discoideum Ariadne-like ubiquitin ligase (RbrA). RbrA may act as an E3 ubiquitin-protein ligase that appears to be required for normal cell-type proportioning and cell sorting during multicellular development, and is also necessary for spore cell viability. Members of this subfamily contain an RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination.


Pssm-ID: 438287  Cd Length: 57  Bit Score: 34.66  E-value: 8.71e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 257196179 489 CTLCHERLEDTHF-VQCpsvpSHKFCFPCSRQ----SIKQQGASGEVYCPsGEKCPLV 541
Cdd:cd16625    3 CPICCDDGELETFsLEC----GHEFCVDCYSQyltsKIKEEGEGCRITCP-GEKCNLI 55
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 489-533 9.39e-03

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 34.41  E-value: 9.39e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 257196179   489 CTLCHER-LEDTHFVQCpsvpSHKFCFPCSRQSIKQQGASgevyCP 533
Cdd:smart00184   1 CPICLEEyLKDPVILPC----GHTFCRSCIRKWLESGNNT----CP 38
 
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