NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|41053864|ref|NP_899031|]
View 

zinc finger MIZ domain-containing protein 1 isoform 1 [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
Zmiz1_N pfam18028
Zmiz1 N-terminal tetratricopeptide repeat domain; This is the N-terminal domain found in Zmiz1 ...
 8-100 1.91e-53

Zmiz1 N-terminal tetratricopeptide repeat domain; This is the N-terminal domain found in Zmiz1 proteins (Zinc finger MIZ domain-containing protein 1). Zmiz1 is a direct Notch1 cofactor that heterogeneously regulates Notch target genes. Zmiz1 directly interacts with the RAM1 domain of Notch1 through this N-terminal tetratricopeptide repeat (TPR) domain. Furthermore, it has been shown that Zmiz1 and Notch1 cooperatively recruit each other to chromatin through direct interaction via the N-terminal TPR domain resulting in a slight increase in activating histone marks and decrease of repressive histone marks. Functional analysis indicate that the N-Terminal Domain of Zmiz1 is important for driving Myc transcription and proliferation indirectly.


:

Pssm-ID: 375500  Cd Length: 93  Bit Score: 181.23  E-value: 1.91e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864      8 IQQTNDRLQCIKQHLQNPANFHNAATELLDWCGDPRAFQRPFEQSLMGCLTVVSRVAAQQGFDLDLGYRLLAVCAANRDK 87
Cdd:pfam18028    1 VQQNNDRLQSIKQHLQNPANFHNACTELLDWCGDPRAFQRPFEQNLLGCLTVVVRVATQQGFDLDLAYRLLAVCAANRKL 80

                           90
                   ....*....|...
gi 41053864     88 FTPKSAALLSSWC 100
Cdd:pfam18028   81 LSPKSAALINRWC 93
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 744-807 1.93e-42

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; 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 different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are 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 enable efficient transfer of ubiquitin from E2 to the substrates.


The actual alignment was detected with superfamily member cd16822:

Pssm-ID: 473075  Cd Length: 64  Bit Score: 148.67  E-value: 1.93e-42
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41053864  744 KVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMW 807
Cdd:cd16822    1 KVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMW 64
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 119-546 4.17e-08

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 4.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   119 PPGKLPMQPPLSSMSsmkPTLSHSDGSFPYDSVPWQQNTNQPPG---SLSVVTTVWGVTNTSQSQVLG----------NP 185
Cdd:PHA03247 2618 PPDTHAPDPPPPSPS---PAANEPDPHPPPTVPPPERPRDDPAPgrvSRPRRARRLGRAAQASSPPQRprrraarptvGS 2694

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   186 MANANNPMNPGGNPMAS--GMSTSNPGINSPQFAGQQQQfSTKAGPAQPYIqPNMYGRPGYPGSGGFGASyPGGPSAPAG 263
Cdd:PHA03247 2695 LTSLADPPPPPPTPEPAphALVSATPLPPGPAAARQASP-ALPAAPAPPAV-PAGPATPGGPARPARPPT-TAGPPAPAP 2771

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   264 MGIPPHTRPPADFTQPAAAAAAAAVAAAAATATATATATVAALQETQNKDINQYGPVCSsfqmgPTQAYNSQFMNQPGPR 343
Cdd:PHA03247 2772 PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP-----PTSAQPTAPPPPPGPP 2846

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   344 GPA-SMGGSLNPAGMAAGMTPSGmSGPPMGMNQPRPPGispfgthgQRMPQ-QTYPGPRPQSLPIQSIKRPYPgepnygn 421
Cdd:PHA03247 2847 PPSlPLGGSVAPGGDVRRRPPSR-SPAAKPAAPARPPV--------RRLARpAVSRSTESFALPPDQPERPPQ------- 2910

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   422 qqygPNSQFPTQPgQYPTPNPPRPLTSPNYPGQ-RMPSQPSTGQYPPPTVNmgqyykPEQFNGQNNTFSSGSSYSSYSQG 500
Cdd:PHA03247 2911 ----PQAPPPPQP-QPQPPPPPQPQPPPPPPPRpQPPLAPTTDPAGAGEPS------GAVPQPWLGALVPGRVAVPRFRV 2979

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 41053864   501 SVNRPPRPVPVAnyPHSPVPGNPTPPMTPGSS--------IPPYLSPSQDVKPP 546
Cdd:PHA03247 2980 PQPAPSREAPAS--STPPLTGHSLSRVSSWASslalheetDPPPVSLKQTLWPP 3031
 
Name Accession Description Interval E-value
Zmiz1_N pfam18028
Zmiz1 N-terminal tetratricopeptide repeat domain; This is the N-terminal domain found in Zmiz1 ...
 8-100 1.91e-53

Zmiz1 N-terminal tetratricopeptide repeat domain; This is the N-terminal domain found in Zmiz1 proteins (Zinc finger MIZ domain-containing protein 1). Zmiz1 is a direct Notch1 cofactor that heterogeneously regulates Notch target genes. Zmiz1 directly interacts with the RAM1 domain of Notch1 through this N-terminal tetratricopeptide repeat (TPR) domain. Furthermore, it has been shown that Zmiz1 and Notch1 cooperatively recruit each other to chromatin through direct interaction via the N-terminal TPR domain resulting in a slight increase in activating histone marks and decrease of repressive histone marks. Functional analysis indicate that the N-Terminal Domain of Zmiz1 is important for driving Myc transcription and proliferation indirectly.


Pssm-ID: 375500  Cd Length: 93  Bit Score: 181.23  E-value: 1.91e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864      8 IQQTNDRLQCIKQHLQNPANFHNAATELLDWCGDPRAFQRPFEQSLMGCLTVVSRVAAQQGFDLDLGYRLLAVCAANRDK 87
Cdd:pfam18028    1 VQQNNDRLQSIKQHLQNPANFHNACTELLDWCGDPRAFQRPFEQNLLGCLTVVVRVATQQGFDLDLAYRLLAVCAANRKL 80

                           90
                   ....*....|...
gi 41053864     88 FTPKSAALLSSWC 100
Cdd:pfam18028   81 LSPKSAALINRWC 93
SP-RING_ZMIZ1 cd16822
SP-RING finger found in zinc finger MIZ domain-containing protein 1 (Zmiz1) and similar ...
 744-807 1.93e-42

SP-RING finger found in zinc finger MIZ domain-containing protein 1 (Zmiz1) and similar proteins; Zmiz1, also known as PIAS-like protein Zimp10 (zinc finger-containing, Miz1, PIAS-like protein on chromosome 10) or retinoic acid-induced protein 17, is a novel PIAS-like protein that was initially identified as an androgen receptor (AR) interacting protein and functions as a transcriptional co-activator. It co-localizes with AR and small ubiquitin-like modifier SUMO-1, forms a protein complex at replication foci in the nucleus, and augments AR-mediated transcription. It also functions as a transcriptional co-activator of the p53 tumor suppressor that plays a critical role in cell cycle progression, DNA repair, and apoptosis. Moreover, Zmiz1 dysfunction may be associated with multiple autoimmune diseases and it has been implicated in the development, function, and survival of melanocytes. Zmiz1 also interacts with Smad3/4 proteins and augments Smad-mediated transcription, suggesting it is important in the regulation of the transforming growth factor beta (TGF-beta)/Smad signaling pathway and may have an inhibitory effect on the immune system. Zmiz1 is overexpressed in a significant percentage of human cutaneous squamous cell carcinoma (SCC), breast, ovarian, and colon cancers, suggesting it may play a broader role in epithelial cancers. It functionally interacts with NOTCH1 to promote C-MYC transcription and activity, and thus is involved in a variety of C-MYC-driven cancers. Zmiz1 contains a PAT domain, a highly conserved Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, also known as msx-interacting zinc finger (Miz domain), and a putative nuclear localization sequence (NLS), as well as a strong intrinsic transactivation domain within the C-terminus. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438471  Cd Length: 64  Bit Score: 148.67  E-value: 1.93e-42
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41053864  744 KVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMW 807
Cdd:cd16822    1 KVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMW 64
zf-MIZ pfam02891
MIZ/SP-RING zinc finger; This domain has SUMO (small ubiquitin-like modifier) ligase activity ...
 745-793 2.97e-22

MIZ/SP-RING zinc finger; This domain has SUMO (small ubiquitin-like modifier) ligase activity and is involved in DNA repair and chromosome organization.


Pssm-ID: 460741  Cd Length: 50  Bit Score: 90.40  E-value: 2.97e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 41053864    745 VSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNK 793
Cdd:pfam02891    1 VSLKCPISYLRISIPVRGRFCKHLQCFDLLSYLESNERTPTWNCPVCDK 49
PHA03247 PHA03247
large tegument protein UL36; Provisional
 119-546 4.17e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 4.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   119 PPGKLPMQPPLSSMSsmkPTLSHSDGSFPYDSVPWQQNTNQPPG---SLSVVTTVWGVTNTSQSQVLG----------NP 185
Cdd:PHA03247 2618 PPDTHAPDPPPPSPS---PAANEPDPHPPPTVPPPERPRDDPAPgrvSRPRRARRLGRAAQASSPPQRprrraarptvGS 2694

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   186 MANANNPMNPGGNPMAS--GMSTSNPGINSPQFAGQQQQfSTKAGPAQPYIqPNMYGRPGYPGSGGFGASyPGGPSAPAG 263
Cdd:PHA03247 2695 LTSLADPPPPPPTPEPAphALVSATPLPPGPAAARQASP-ALPAAPAPPAV-PAGPATPGGPARPARPPT-TAGPPAPAP 2771

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   264 MGIPPHTRPPADFTQPAAAAAAAAVAAAAATATATATATVAALQETQNKDINQYGPVCSsfqmgPTQAYNSQFMNQPGPR 343
Cdd:PHA03247 2772 PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP-----PTSAQPTAPPPPPGPP 2846

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   344 GPA-SMGGSLNPAGMAAGMTPSGmSGPPMGMNQPRPPGispfgthgQRMPQ-QTYPGPRPQSLPIQSIKRPYPgepnygn 421
Cdd:PHA03247 2847 PPSlPLGGSVAPGGDVRRRPPSR-SPAAKPAAPARPPV--------RRLARpAVSRSTESFALPPDQPERPPQ------- 2910

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   422 qqygPNSQFPTQPgQYPTPNPPRPLTSPNYPGQ-RMPSQPSTGQYPPPTVNmgqyykPEQFNGQNNTFSSGSSYSSYSQG 500
Cdd:PHA03247 2911 ----PQAPPPPQP-QPQPPPPPQPQPPPPPPPRpQPPLAPTTDPAGAGEPS------GAVPQPWLGALVPGRVAVPRFRV 2979

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 41053864   501 SVNRPPRPVPVAnyPHSPVPGNPTPPMTPGSS--------IPPYLSPSQDVKPP 546
Cdd:PHA03247 2980 PQPAPSREAPAS--STPPLTGHSLSRVSSWASslalheetDPPPVSLKQTLWPP 3031
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 125-484 5.89e-08

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 56.94  E-value: 5.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    125 MQPPLSSMSSMKPTLSHsdgsfPYDSVPWQQNTNQPPGSLSVVTTVWGVTNTSQSQvlgNPMA----NANNPMNPGGN-- 198
Cdd:pfam09606  149 MQPGGQAGGMMQPSSGQ-----PGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQ---MPPQmgvpGMPGPADAGAQmg 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    199 ---PMASGMSTSNPGINSPQFAGQQQQFSTKAGPAQPYIQPNMYGRPGYPGSGGFGASYPGGPsapagmGIPPHTRPPAd 275
Cdd:pfam09606  221 qqaQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQP------MGPPGQQPGA- 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    276 ftQPAAAAAAAAVAAAAATATATATATVAALQETQNKDINQygPVCSSFQMGPTQAYNSQFMNQPGPRGPASMGGslnpa 355
Cdd:pfam09606  294 --MPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQ--SVGQGGQVVALGGLNHLETWNPGNFGGLGANP----- 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    356 gmaAGMTPSGMsgppMGMNQPRPPGISPFGTHGQRMPQQtypgprpqslpiQSIKRPYPGEPNYGNQQYGPNSQFPTqPG 435
Cdd:pfam09606  365 ---MQRGQPGM----MSSPSPVPGQQVRQVTPNQFMRQS------------PQPSVPSPQGPGSQPPQSHPGGMIPS-PA 424

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 41053864    436 QYPTPNPPrplTSPNYPGQRMPSQPSTGQyppPTVNMGQYYKPEQFNGQ 484
Cdd:pfam09606  425 LIPSPSPQ---MSQQPAQQRTIGQDSPGG---SLNTPGQSAVNSPLNPQ 467
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 371-470 4.16e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 44.41  E-value: 4.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    371 MGMNQPrpPGISPF-GTHGQRM-----PQQTYPGpRPQSLPIQSiKRPYPGEPNYGNQ-----QYGPNSQFPTQPGQYPT 439
Cdd:TIGR01628  380 PRMRQL--PMGSPMgGAMGQPPyygqgPQQQFNG-QPLGWPRMS-MMPTPMGPGGPLRpnglaPMNAVRAPSRNAQNAAQ 455

                           90       100       110
                   ....*....|....*....|....*....|.
gi 41053864    440 PNPPRPLTSPnyPGQRMPSQPSTGQYPPPTV 470
Cdd:TIGR01628  456 KPPMQPVMYP--PNYQSLPLSQDLPQPQSTA 484
 
Name Accession Description Interval E-value
Zmiz1_N pfam18028
Zmiz1 N-terminal tetratricopeptide repeat domain; This is the N-terminal domain found in Zmiz1 ...
 8-100 1.91e-53

Zmiz1 N-terminal tetratricopeptide repeat domain; This is the N-terminal domain found in Zmiz1 proteins (Zinc finger MIZ domain-containing protein 1). Zmiz1 is a direct Notch1 cofactor that heterogeneously regulates Notch target genes. Zmiz1 directly interacts with the RAM1 domain of Notch1 through this N-terminal tetratricopeptide repeat (TPR) domain. Furthermore, it has been shown that Zmiz1 and Notch1 cooperatively recruit each other to chromatin through direct interaction via the N-terminal TPR domain resulting in a slight increase in activating histone marks and decrease of repressive histone marks. Functional analysis indicate that the N-Terminal Domain of Zmiz1 is important for driving Myc transcription and proliferation indirectly.


Pssm-ID: 375500  Cd Length: 93  Bit Score: 181.23  E-value: 1.91e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864      8 IQQTNDRLQCIKQHLQNPANFHNAATELLDWCGDPRAFQRPFEQSLMGCLTVVSRVAAQQGFDLDLGYRLLAVCAANRDK 87
Cdd:pfam18028    1 VQQNNDRLQSIKQHLQNPANFHNACTELLDWCGDPRAFQRPFEQNLLGCLTVVVRVATQQGFDLDLAYRLLAVCAANRKL 80

                           90
                   ....*....|...
gi 41053864     88 FTPKSAALLSSWC 100
Cdd:pfam18028   81 LSPKSAALINRWC 93
SP-RING_ZMIZ1 cd16822
SP-RING finger found in zinc finger MIZ domain-containing protein 1 (Zmiz1) and similar ...
 744-807 1.93e-42

SP-RING finger found in zinc finger MIZ domain-containing protein 1 (Zmiz1) and similar proteins; Zmiz1, also known as PIAS-like protein Zimp10 (zinc finger-containing, Miz1, PIAS-like protein on chromosome 10) or retinoic acid-induced protein 17, is a novel PIAS-like protein that was initially identified as an androgen receptor (AR) interacting protein and functions as a transcriptional co-activator. It co-localizes with AR and small ubiquitin-like modifier SUMO-1, forms a protein complex at replication foci in the nucleus, and augments AR-mediated transcription. It also functions as a transcriptional co-activator of the p53 tumor suppressor that plays a critical role in cell cycle progression, DNA repair, and apoptosis. Moreover, Zmiz1 dysfunction may be associated with multiple autoimmune diseases and it has been implicated in the development, function, and survival of melanocytes. Zmiz1 also interacts with Smad3/4 proteins and augments Smad-mediated transcription, suggesting it is important in the regulation of the transforming growth factor beta (TGF-beta)/Smad signaling pathway and may have an inhibitory effect on the immune system. Zmiz1 is overexpressed in a significant percentage of human cutaneous squamous cell carcinoma (SCC), breast, ovarian, and colon cancers, suggesting it may play a broader role in epithelial cancers. It functionally interacts with NOTCH1 to promote C-MYC transcription and activity, and thus is involved in a variety of C-MYC-driven cancers. Zmiz1 contains a PAT domain, a highly conserved Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, also known as msx-interacting zinc finger (Miz domain), and a putative nuclear localization sequence (NLS), as well as a strong intrinsic transactivation domain within the C-terminus. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438471  Cd Length: 64  Bit Score: 148.67  E-value: 1.93e-42
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41053864  744 KVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMW 807
Cdd:cd16822    1 KVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMW 64
SP-RING_ZMIZ2 cd16823
SP-RING finger found in zinc finger MIZ domain-containing protein 2 (Zmiz2) and similar ...
 739-799 1.33e-38

SP-RING finger found in zinc finger MIZ domain-containing protein 2 (Zmiz2) and similar proteins; Zmiz2, also known as PIAS-like protein Zimp7 (zinc finger-containing, Miz1, PIAS-like protein on chromosome 7), is a novel PIAS-like protein that was initially identified as an androgen receptor (AR) interacting protein and functions as a transcriptional co-activator. It interacts with beta-catenin and enhances Wnt/beta-catenin-mediated transcription. It also associates with BRG1 and BAF57, components of the ATP-dependent mammalian SWI/SNF-like BAF chromatin-remodeling complexes, and thus plays a potential role in modulation of AR and/or other nuclear receptor-mediated transcription. For instance, it can increase the effects of BRG1 on AR-mediated transcriptional activity. Moreover, Zmiz2 physically interacts with PIAS proteins, especially PIAS3. Through this interaction, PIAS3 augments Zmiz2-mediated transcription, suggesting PIAS proteins may play a regulatory role in Zmiz-mediated transcription. Furthermore, Zmiz2 is involved in transcriptional regulation of factors essential for patterning in the dorsoventral axis. It is required for the restriction of the zebrafish organizer and mesoderm development. Zmiz2 contains a PAT domain, a highly conserved Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, also known as msx-interacting zinc finger (Miz domain), and a strong intrinsic transactivation domain within the C-terminus. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438472  Cd Length: 61  Bit Score: 137.49  E-value: 1.33e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41053864  739 EQTAIKVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEG 799
Cdd:cd16823    1 EQTAIKVSLKCPITFRRIQLPARGHDCRHIQCFDLESYLQLNCERGTWRCPVCNKTALLEG 61
SP-RING_ZMIZ cd16791
SP-RING finger found in zinc finger MIZ domain-containing protein Zmiz1, Zmiz2, and similar ...
 746-793 1.03e-32

SP-RING finger found in zinc finger MIZ domain-containing protein Zmiz1, Zmiz2, and similar proteins; This subfamily includes Zmiz1 (Zimp10) and its homolog Zmiz2 (Zimp7), both initially identified in humans as androgen receptor (AR) interacting proteins which function as transcriptional co-activators. They interact with BRG1, the catalytic subunit of the SWI-SNF remodeling complex. They also associate with other hormone nuclear receptors and transcription factors, such as p53 and Smad3/Smad4, and regulate transcription of specific target genes by altering their chromatin structure. This subfamily also includes tonalli (Tna), an ortholog identified in Drosophila. It genetically interacts with the ATP-dependent SWI/SNF and Mediator complexes, suggesting a potential role for the Zmiz proteins in chromatin remodeling. Zmiz proteins contain a highly conserved Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, also known as msx-interacting zinc finger (Miz domain), and a strong transactivation domain within the C-terminus. The SP-RING/Miz domain is highly conserved in members of the PIAS family and confers SUMO-conjugating activity. It is a variant of the RING finger, and lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers. The strong intrinsic transactivation domain facilitates Zmiz proteins to augment the transcriptional activity of nuclear hormone receptors and other transcriptional factors. They may act as transcriptional co-regulators.


Pssm-ID: 438445  Cd Length: 48  Bit Score: 120.30  E-value: 1.03e-32
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 41053864  746 SLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNK 793
Cdd:cd16791    1 SLKCPITFRRITLPARGHDCKHIQCFDLESYLQLNCERGTWRCPVCNK 48
SP-RING_PIAS-like cd16650
SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases; The SP-RING ...
 746-793 3.24e-25

SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases; The SP-RING family includes PIAS (protein inhibitor of activated STAT) proteins, Zmiz proteins, and Siz proteins from plants and fungi. PIAS proteins modulate the activity of several transcription factors and act as E3 ubiquitin ligases in the sumoylation pathway. There are four members: PIAS1, PIAS2 (also known as PIASx), PIAS3, and PIAS4 (also known as PIASy). PIAS proteins were initially identified as inhibitors of activated STAT only, but are now known to interact with and modulate several other proteins, including androgen receptor (AR), tumor suppressor p53, and the transforming growth factor-beta (TGF-beta) signaling protein SMAD. They interact with STATs in a cytokine-dependent manner. PIAS proteins have SUMO E3-ligase activity and interaction of PIAS proteins with transcription factors often results in sumoylation of that protein. Zmiz1 (Zimp10) and its homolog Zmiz2 (Zimp7) were initially identified in humans as androgen receptor (AR) interacting proteins that function as transcriptional co-activators. They interact with BRG1, the catalytic subunit of the SWI-SNF remodeling complex. They also associate with other hormone nuclear receptors and transcription factors such as p53 and Smad3/Smad4, and regulate transcription of specific target genes by altering their chromatin structure. SIZ1 proteins from plants and fungi are also founding members of this family. SIZ1-mediated conjugation of SUMO1 and SUMO2 to other intracellular proteins is essential in Arabidopsis. Yeast SIZ proteins are SUMO E3 ligases involved in a novel pathway of chromosome maintenance. They enhance SUMO modification to many substrates in vivo, but also exhibit unique substrate specificity. PIAS proteins contain a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, which is essential for SUMO ligase activity. The SP-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438312  Cd Length: 48  Bit Score: 98.88  E-value: 3.24e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 41053864  746 SLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNK 793
Cdd:cd16650    1 SLRCPLSLKRIKTPARGKHCKHLQCFDLDSYLEFNKRKPTWKCPICDK 48
zf-MIZ pfam02891
MIZ/SP-RING zinc finger; This domain has SUMO (small ubiquitin-like modifier) ligase activity ...
 745-793 2.97e-22

MIZ/SP-RING zinc finger; This domain has SUMO (small ubiquitin-like modifier) ligase activity and is involved in DNA repair and chromosome organization.


Pssm-ID: 460741  Cd Length: 50  Bit Score: 90.40  E-value: 2.97e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 41053864    745 VSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNK 793
Cdd:pfam02891    1 VSLKCPISYLRISIPVRGRFCKHLQCFDLLSYLESNERTPTWNCPVCDK 49
SP-RING_Siz-like cd16792
SP-RING finger found in Arabidopsis thaliana E3 SUMO-protein ligase SIZ1 (AtSIZ1) and similar ...
 746-794 1.31e-19

SP-RING finger found in Arabidopsis thaliana E3 SUMO-protein ligase SIZ1 (AtSIZ1) and similar proteins; SIZ1-mediated conjugation of SUMO1 and SUMO2 to other intracellular proteins is essential in Arabidopsis. AtSIZ1 negatively regulates abscisic acid (ABA) signaling through the sumoylation of bZIP transcripton factor ABI5. It also mediates sumoylation of bromodomain GTE proteins. Moreover, AtSIZ1 regulates flowering by controlling a salicylic acid-mediated floral promotion pathway and through affecting on FLOWERING LOCUS C (FLC) chromatin structure. It also plays a role in drought stress response likely through the regulation of gene expression. Members of this subfamily contain an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box, a plant homeodomain (PHD) finger, and a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438446  Cd Length: 50  Bit Score: 83.23  E-value: 1.31e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 41053864  746 SLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKT 794
Cdd:cd16792    1 SLKCPLSYSRIKVPCRSIKCTHIQCFDLDSFLQLNEQTPSWQCPICNKN 49
SP-RING-like cd16452
SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a ...
 747-792 1.26e-15

SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a group of proteins with variants of RING fingers that are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers. They include SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases and SPL-RING finger found in E3 SUMO-protein ligase NSE2. The SP-RING family includes PIAS (protein inhibitor of activated STAT) proteins, Zmiz proteins, and Siz proteins from plants and fungi. The PIAS (protein inhibitor of activated STAT) protein family modulates the activity of several transcription factors and acts as an E3 ubiquitin ligase in the sumoylation pathway. NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress.


Pssm-ID: 438116 [Multi-domain]  Cd Length: 45  Bit Score: 71.52  E-value: 1.26e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 41053864  747 LKCPITFRRIQLPARGHDCKHvqCFDLESYLQLNCER-GTWRCPVCN 792
Cdd:cd16452    1 LKCPITQKRMKDPVRGKHCGH--CFDLEAILQYLKRRkKKWKCPVCS 45
SP-RING_PIAS2 cd16819
SP-RING finger found in protein inhibitor of activated STAT protein 2 (PIAS2) and similar ...
 741-800 1.20e-13

SP-RING finger found in protein inhibitor of activated STAT protein 2 (PIAS2) and similar proteins; PIAS2, also known as androgen receptor-interacting protein 3 (ARIP3), DAB2-interacting protein (DIP), Msx-interacting zinc finger protein (Miz1), PIAS-NY protein, protein inhibitor of activated STAT x, protein inhibitor of activated STAT2, is an E3 SUMO-protein ligase highly expressed in the testis. It functions as a transcriptional activator of BCL2 and is essential for blocking c-MYC-induced apoptosis. It also acts as a negative regulator of cell proliferation, induces expression of the cell-cycle inhibitors p15(Ink4b) and p21(Cip1), and activates transcription of the p21(Cip1) gene in response to UV irradiation. Moreover, PIAS2 associates with topoisomerase II binding protein 1 (TopBP1), an essential activator of the Atr kinase. It thus affects the activity of the Atr checkpoint. Receptor of activated C kinase 1 (RACK1), glucocorticoid receptor (GR)-interacting protein 1 (GRIP1), friend leukemia integration-I (FLI-1), and ubiquitously expressed transcript (UXT) are binding partners of PIAS2. The interaction between UXT and PIAS2 may be important for the transcriptional activation of androgen receptor (AR). PIAS2 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus, and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and an acidic C-terminal domain. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438468  Cd Length: 60  Bit Score: 66.65  E-value: 1.20e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864  741 TAIKVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGL 800
Cdd:cd16819    1 TSLRVSLMCPLGKMRLTIPCRAVTCSHLQCFDAALYLQMNEKKPTWICPVCDKKAAYESL 60
SP-RING_PIAS4 cd16821
SP-RING finger found in protein inhibitor of activated STAT protein 4 (PIAS4) and similar ...
 741-798 1.64e-12

SP-RING finger found in protein inhibitor of activated STAT protein 4 (PIAS4) and similar proteins; PIAS4, also known as PIASy or protein inhibitor of activated STAT protein gamma (PIAS-gamma), is an E3 SUMO-protein ligase that interacts with the androgen receptor (AR) and is involved in ubiquitin signaling pathways. It is associated with macro/microcephaly in the novel interstitial 19p13.3 microdeletion/microduplication syndrome. It also regulates the hypoxia signalling pathway by interacting with the tumor suppressor von Hippel-Lindau (VHL), which leads to VHL sumoylation, oligomerization, and impaired function during growth of pancreatic cancer cells. Moreover, PIAS4 acts as a direct binding partner for vitamin D receptor (VDR) and facilitates its modification with SUMO2. The process of SUMOylation modulates VDR-mediated signaling. As components of the DNA-damage response (DDR), PIAS4 together with PIAS1 promote responses to DNA double-strand breaks (DSBs). They are required for effective ubiquitin-adduct formation mediated by RNF8, RNF168, and BRCA1 at sites of DNA damage. PIAS4 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and an acidic C-terminal domain. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438470  Cd Length: 58  Bit Score: 63.15  E-value: 1.64e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 41053864  741 TAIKVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLE 798
Cdd:cd16821    1 TGVRVSLICPLVKMRLSVPCRAETCAHLQCFDAVFYLQMNEKKPTWTCPVCDKPAPYD 58
SP-RING_PIAS3 cd16820
SP-RING finger found in protein inhibitor of activated STAT protein 3 (PIAS3) and similar ...
 741-800 3.48e-12

SP-RING finger found in protein inhibitor of activated STAT protein 3 (PIAS3) and similar proteins; PIAS3 is an E3 SUMO-protein ligase that was initially identified as an interleukin-6 (IL-6)-dependent repressor of signal transducer and activator of transcription 3 (STAT3) and has anti-proliferative properties. It binds specifically to phosphorylated STAT3 and inhibits its transcriptional activity by blocking its binding to DNA. It regulates STAT3-mediated induction of Snail expression, as well as suppresses acute graft-versus-host disease (GVHD) by modulating effector T and B cell subsets through inhibition of STAT3 activation. It activates the intrinsic apoptotic pathway in non-small cell lung cancer cells independent of p53 status. When overexpressed, it can interact with STAT5 to regulate prolactin-induced STAT5-mediated gene expression. Moreover, PIAS3 binds to and activates Smad3 transcriptional activity, resulting in the enhancement of transforming growth factor-beta (TGF-beta) signaling. It functions as a transcriptional corepressor of Erythroid Kruppel-like factor (EKLF or KLF1) and thus plays an important role in erythropoiesis. It also plays a significant role in the DNA damage response (DDR) pathway by promoting homologous recombination (HR)- and non-homologous end joining (NHEJ)-mediated DNA double-strand break (DSB) repair. Furthermore, PIAS3 preferentially interacts with and enhances the SUMOylation of TAK1-binding protein 2 (TAB2), an upstream adaptor protein in the IL-1 signaling pathway. It also promotes SUMOylation and nuclear sequestration of ErbB4 receptor tyrosine kinase. In addition, PIAS3 may form a complex with microphthalmia-associated transcription factor, nuclear factor-kappaB, Smad, and estrogen receptor. Its other transcription factor binding partners include: ETS, EGR1, NR1I2, and GATA1. PIAS3 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and an acidic C-terminal domain. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438469  Cd Length: 62  Bit Score: 62.37  E-value: 3.48e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864  741 TAIKVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGL 800
Cdd:cd16820    1 TSLRVSLMCPLGKMRLTVPCRAITCTHLQCFDAALYLQMNEKKPTWTCPVCDKKAPYESL 60
SP-RING_PIAS1 cd16818
SP-RING finger found in protein inhibitor of activated STAT protein 1 (PIAS1) and similar ...
 741-800 3.69e-12

SP-RING finger found in protein inhibitor of activated STAT protein 1 (PIAS1) and similar proteins; PIAS1, also known as DEAD/H box-binding protein 1, Gu-binding protein (GBP), or RNA helicase II-binding protein, was initially identified as an inhibitor of STAT1 that blocks the DNA-binding activity of STAT1 and specifically inhibits STAT1-mediated gene transcription in response to cytokine stimulation. It selectively inhibits interferon-inducible gene expression and plays an important role in the IFN-gamma- or IFN-beta-mediated innate immune response through negative regulation of STAT1. It also regulates the activity of other transcription factors to regulate immune response, such as NF-kappaB and Smad4. Moreover, PIAS1 functions as an E3 small ubiquitin-like modifier (SUMO)-protein ligase specifying target proteins for SUMO conjugation by Ubc9. The sumoylation activity of PIAS1 can suppress cytokine transforming growth factor beta (TGFbeta)-induced epithelial mesenchymal transition (EMT) in non-transformed epithelial cells to promote activation of the matrix metalloproteinase 2 (MMP2). It thus regulates TGFbeta-induced cancer cell invasion and metastasis. PIAS1 may also be involved in spatial learning and memory formation through its SUMOylation of cAMP-responsive element binding protein (CREB). In addition, PIAS1 is the E3 ligase responsible for SUMOylation of High mobility group nucleosomal binding domain 2 (HMGN2), which is a small and unique non-histone protein that has many functions in a variety of cellular processes, including regulation of chromatin structure, transcription, and DNA repair, as well as antimicrobial activity, cell homing, and regulating cytokine release. Furthermore, PIAS1 is a genuine chromatin-bound androgen receptor (AR) co-regulator that functions in a target gene selective fashion to regulate prostate cancer cell growth. It also mediates the SUMOylation of c-Myc, which is the most frequently overexpressed oncogene in tumors, including breast cancer, colon cancer, and lung cancer. Necdin, a pleiotropic protein that promotes differentiation and survival of mammalian neurons, can suppress PIAS1 both by inhibiting SUMO E3 ligase activity and by promoting ubiquitin-dependent degradation. PIAS1 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and the acidic C-terminal domain. The SP-RING finger mediates the interaction of PIAS1 with the SUMO E2 conjugating enzyme Ubc9. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438467  Cd Length: 60  Bit Score: 62.38  E-value: 3.69e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864  741 TAIKVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGL 800
Cdd:cd16818    1 TSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHL 60
SP-RING_PIAS cd16790
SP-RING finger found in protein inhibitor of activated signal transducer and activator of ...
 746-793 7.04e-12

SP-RING finger found in protein inhibitor of activated signal transducer and activator of transcription (PIAS) proteins; The PIAS (protein inhibitor of activated STAT) protein family modulates the activity of several transcription factors and acts as an E3 ubiquitin ligase in the sumoylation pathway. It consists of four members: PIAS1, PIAS2 (also known as PIASx), PIAS3, and PIAS4 (also known as PIASy). PIAS proteins were initially identified as inhibitors of activated STAT only, but are now known to interact with and modulate several other proteins, including androgen receptor (AR), tumor suppressor p53, and the transforming growth factor-beta (TGF-beta) signaling protein SMAD. They interact with STATs in a cytokine-dependent manner. PIAS1, PIAS2, and PIAS3 interact with STAT1, STAT3, and STAT4, respectively. In addition, PIAS4 is associated with STAT1. PIAS proteins have SUMO E3-ligase activity and interaction of PIAS proteins with transcription factors often results in sumoylation of that protein. PIAS proteins contain an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, which is required for the trans-repression of STAT1 activity by PIAS2, a PINT motif, which is essential for nuclear retention of PIAS3L (the long form of PIAS3), a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, which is essential for SUMO ligase activity, and the acidic C-terminal domain, which is involved in binding of PIAS3 to the nuclear coactivator TIF2. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438444  Cd Length: 48  Bit Score: 60.98  E-value: 7.04e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 41053864  746 SLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNK 793
Cdd:cd16790    1 SLMCPLGKMRLTIPCRALTCSHLQCFDAALYLQMNEKKPTWICPVCDK 48
SP-RING_ScSiz-like cd16793
SP-RING finger found in Saccharomyces cerevisiae E3 SUMO-protein ligase SIZ1, SIZ2, and ...
 745-791 2.73e-10

SP-RING finger found in Saccharomyces cerevisiae E3 SUMO-protein ligase SIZ1, SIZ2, and similar proteins; Saccharomyces cerevisiae SIZ proteins, also known as SAP and Miz-finger domain-containing proteins, are Siz/PIAS RING (SP-RING) family SUMO E3 ligases, and may be involved in a novel pathway of chromosome maintenance. They enhance SUMO modification with many substrates in vivo, but also exhibit unique substrate specificity. SIZ1, also known as ubiquitin-like protein ligase 1 (Ull1), modifies both cytoplasmic and nuclear proteins. It functions as an E3 factor specific for septin components. SIZ1-dependent substrates include Cdc3 and Cdc11 (septin subunits), Prp45 (a splicing factor), and the proliferating cell nuclear antigen (PCNA). SIZ2, also known as NFI1, interacts with Smt3, SUMO/Smt3 conjugating enzyme Ubc9, and a septin component Cdc3. Members of this subfamily contain an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and an acidic C-terminal domain. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438447  Cd Length: 56  Bit Score: 57.00  E-value: 2.73e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 41053864  745 VSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVC 791
Cdd:cd16793    4 MSLQCPISYTRMKYPSKSINCKHLQCFDALWFLHSQLQIPTWQCPVC 50
PHA03247 PHA03247
large tegument protein UL36; Provisional
 119-546 4.17e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 4.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   119 PPGKLPMQPPLSSMSsmkPTLSHSDGSFPYDSVPWQQNTNQPPG---SLSVVTTVWGVTNTSQSQVLG----------NP 185
Cdd:PHA03247 2618 PPDTHAPDPPPPSPS---PAANEPDPHPPPTVPPPERPRDDPAPgrvSRPRRARRLGRAAQASSPPQRprrraarptvGS 2694

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   186 MANANNPMNPGGNPMAS--GMSTSNPGINSPQFAGQQQQfSTKAGPAQPYIqPNMYGRPGYPGSGGFGASyPGGPSAPAG 263
Cdd:PHA03247 2695 LTSLADPPPPPPTPEPAphALVSATPLPPGPAAARQASP-ALPAAPAPPAV-PAGPATPGGPARPARPPT-TAGPPAPAP 2771

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   264 MGIPPHTRPPADFTQPAAAAAAAAVAAAAATATATATATVAALQETQNKDINQYGPVCSsfqmgPTQAYNSQFMNQPGPR 343
Cdd:PHA03247 2772 PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP-----PTSAQPTAPPPPPGPP 2846

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   344 GPA-SMGGSLNPAGMAAGMTPSGmSGPPMGMNQPRPPGispfgthgQRMPQ-QTYPGPRPQSLPIQSIKRPYPgepnygn 421
Cdd:PHA03247 2847 PPSlPLGGSVAPGGDVRRRPPSR-SPAAKPAAPARPPV--------RRLARpAVSRSTESFALPPDQPERPPQ------- 2910

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   422 qqygPNSQFPTQPgQYPTPNPPRPLTSPNYPGQ-RMPSQPSTGQYPPPTVNmgqyykPEQFNGQNNTFSSGSSYSSYSQG 500
Cdd:PHA03247 2911 ----PQAPPPPQP-QPQPPPPPQPQPPPPPPPRpQPPLAPTTDPAGAGEPS------GAVPQPWLGALVPGRVAVPRFRV 2979

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 41053864   501 SVNRPPRPVPVAnyPHSPVPGNPTPPMTPGSS--------IPPYLSPSQDVKPP 546
Cdd:PHA03247 2980 PQPAPSREAPAS--STPPLTGHSLSRVSSWASslalheetDPPPVSLKQTLWPP 3031
PHA03247 PHA03247
large tegument protein UL36; Provisional
 185-563 4.98e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 4.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   185 PMANANNPmnPGGNPMASGMSTSNPGINSPQFAGQQQQFSTKAGPAQPYIQPNMYGRPGYPGSGGFGASYPGGPSAPAGM 264
Cdd:PHA03247 2631 PSPAANEP--DPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTP 2708

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   265 GIPPHTRPPADFTQPAAAAAAAAVAAAAATATATATATVAALQETQNKDINQ---YGPVCSSFQMGPTQAynsqfmnqPG 341
Cdd:PHA03247 2709 EPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPpttAGPPAPAPPAAPAAG--------PP 2780

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   342 PRGPASMGGSLNPAgMAAGMTPSGMSGPPMGMNQP--------RPPGISPFGTHGQRMPQQTYPGPRPQSLPIQSikRPY 413
Cdd:PHA03247 2781 RRLTRPAVASLSES-RESLPSPWDPADPPAAVLAPaaalppaaSPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGG--SVA 2857

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   414 PGEPnygNQQYGPNSQFPTQPGQYPTPnPPRPLTSPNYPGQRMP-SQPSTGQYPPPTVNMGQYYKPEqfngqnntfssgs 492
Cdd:PHA03247 2858 PGGD---VRRRPPSRSPAAKPAAPARP-PVRRLARPAVSRSTESfALPPDQPERPPQPQAPPPPQPQ------------- 2920

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41053864   493 syssysqgsvnrPPRPVPVANYPHSPVPGNPTPPMTPGSSIPPYLSPSQDVKPPFPPDIKPNMSALP----PPPA 563
Cdd:PHA03247 2921 ------------PQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPrfrvPQPA 2983
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 125-484 5.89e-08

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 56.94  E-value: 5.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    125 MQPPLSSMSSMKPTLSHsdgsfPYDSVPWQQNTNQPPGSLSVVTTVWGVTNTSQSQvlgNPMA----NANNPMNPGGN-- 198
Cdd:pfam09606  149 MQPGGQAGGMMQPSSGQ-----PGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQ---MPPQmgvpGMPGPADAGAQmg 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    199 ---PMASGMSTSNPGINSPQFAGQQQQFSTKAGPAQPYIQPNMYGRPGYPGSGGFGASYPGGPsapagmGIPPHTRPPAd 275
Cdd:pfam09606  221 qqaQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQP------MGPPGQQPGA- 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    276 ftQPAAAAAAAAVAAAAATATATATATVAALQETQNKDINQygPVCSSFQMGPTQAYNSQFMNQPGPRGPASMGGslnpa 355
Cdd:pfam09606  294 --MPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQ--SVGQGGQVVALGGLNHLETWNPGNFGGLGANP----- 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    356 gmaAGMTPSGMsgppMGMNQPRPPGISPFGTHGQRMPQQtypgprpqslpiQSIKRPYPGEPNYGNQQYGPNSQFPTqPG 435
Cdd:pfam09606  365 ---MQRGQPGM----MSSPSPVPGQQVRQVTPNQFMRQS------------PQPSVPSPQGPGSQPPQSHPGGMIPS-PA 424

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 41053864    436 QYPTPNPPrplTSPNYPGQRMPSQPSTGQyppPTVNMGQYYKPEQFNGQ 484
Cdd:pfam09606  425 LIPSPSPQ---MSQQPAQQRTIGQDSPGG---SLNTPGQSAVNSPLNPQ 467
PHA03247 PHA03247
large tegument protein UL36; Provisional
 192-562 6.14e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.26  E-value: 6.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   192 PMNPGGNPMASGMSTSNP----GINSPQFAGQQQQFSTKAGPAQPYIQPNMYGRPGYPGSGGF-----GASYPGGPSAPA 262
Cdd:PHA03247 2601 PVDDRGDPRGPAPPSPLPpdthAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRprrarRLGRAAQASSPP 2680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   263 GMGIPPHTRPP----ADFTQPAAAAAAAAVAAAAATATATATAtvaalqetqnkdinqygpvcssfqmGPTQAYNSQFMN 338
Cdd:PHA03247 2681 QRPRRRAARPTvgslTSLADPPPPPPTPEPAPHALVSATPLPP-------------------------GPAAARQASPAL 2735

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   339 QPGPRGPASMGGSLNPAGMAAGMTPSGMSGPPmgmnQPRPPGISPFGthgqrmPQQTYPGPRPQSLPIQSIKRPYPGEPn 418
Cdd:PHA03247 2736 PAAPAPPAVPAGPATPGGPARPARPPTTAGPP----APAPPAAPAAG------PPRRLTRPAVASLSESRESLPSPWDP- 2804

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   419 ygnqQYGPNSQFPTQPGQYPTPNPPRPLTSPNYPGQRMPSQPStgQYPPPTVNMGQYYKP----EQFNGQNNTFSSGSSY 494
Cdd:PHA03247 2805 ----ADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP--GPPPPSLPLGGSVAPggdvRRRPPSRSPAAKPAAP 2878

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41053864   495 SSYSQGSVNRPPRPVPVANYPHSPVPgnPTPPMTPGSSIPPYLSPSQDVKP-PFPPDIKPNMSALPPPP 562
Cdd:PHA03247 2879 ARPPVRRLARPAVSRSTESFALPPDQ--PERPPQPQAPPPPQPQPQPPPPPqPQPPPPPPPRPQPPLAP 2945
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
 747-807 1.10e-07

SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Moreover, NSE2 together with its partner proteins SMC6 and SMC5 form a tight subcomplex of the structural maintenance of chromosomes SMC5-6 complex, which includes another two subcomplexes, NSE1-NSE3-NSE4 and NSE5-NSE6. SMC6 and NSE3 are sumoylated in an NSE2-dependent manner, but SMC5 and NSE1 are not. NSE2-dependent E3 SUMO ligase activity is required for efficient DNA repair, but not for SMC5-6 complex stability. NSE2 contains a RING variant known as a Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription)-like RING (SPL-RING) finger that is likely shared by the SP-RING type SUMO E3 ligases, such as PIAS family proteins. The SPL-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It harbors only one Zn binding site and is required for the sumoylating activity.


Pssm-ID: 438313 [Multi-domain]  Cd Length: 67  Bit Score: 49.57  E-value: 1.10e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41053864  747 LKCPITFRRIQLPARGHDCKHVqcFDLESYLQ-LNCERGTWRCPV--CNKTALLEGLEVDQYMW 807
Cdd:cd16651    1 LKCPITQQLMVDPVRNKKCGHT--YEKAAILQyLQSRKKKAKCPVagCRNTVSKSDLVPDPELK 62
PHA03378 PHA03378
EBNA-3B; Provisional
 342-578 3.75e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 51.22  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   342 PRGPASMggSLNPAGMAAGMTPSGMSGPPMGMNQPRPpgiSPFGTHGQRMPQQTypgPRPQSLPIQSiKRPYPGEPNYGN 421
Cdd:PHA03378  606 PEPPTTQ--SHIPETSAPRQWPMPLRPIPMRPLRMQP---ITFNVLVFPTPHQP---PQVEITPYKP-TWTQIGHIPYQP 676

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   422 QQYGPNSQFPTQ--PGQY-PTPNPPRPLTSPNY-PGQRMPSQPSTGQYPPPTVNMGQYYKPEQFNGQnntfssgsSYSSY 497
Cdd:PHA03378  677 SPTGANTMLPIQwaPGTMqPPPRAPTPMRPPAApPGRAQRPAAATGRARPPAAAPGRARPPAAAPGR--------ARPPA 748

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   498 SQGSVNRPPRPVPVANYPHSPVPGNPTPPMTPGSSIPPYLSPSQDVKPPFPPDIKPNMSALPPP-------PANHNDELR 570
Cdd:PHA03378  749 AAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRaapgqqgPTKQILRQL 828


                  ....*...
gi 41053864   571 LTFPVRDG 578
Cdd:PHA03378  829 LTGGVKRG 836
PHA03247 PHA03247
large tegument protein UL36; Provisional
 339-563 7.52e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 7.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   339 QPGPR--GPASMGGSLN---PAGMAAGMTPSGMSGPPMGMNQPRPPgisPFGTHGQRMPQqtyPGPRPQ-SLPIQSIKRP 412
Cdd:PHA03247 2572 RPAPRpsEPAVTSRARRpdaPPQSARPRAPVDDRGDPRGPAPPSPL---PPDTHAPDPPP---PSPSPAaNEPDPHPPPT 2645

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   413 YPGEPNYGNQQYGPNSQFP------------TQPGQYPTPNPPRPLTSPNYPGQRMPSQPSTGQYPPPTVNMGQYYKP-E 479
Cdd:PHA03247 2646 VPPPERPRDDPAPGRVSRPrrarrlgraaqaSSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPgP 2725

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   480 QFNGQNNTFSSGSSYSSYSQGSVNRPPRPVPVANYPHSPVPGNPTPPMTPGSSIPPYLSPSQDVK-------PPFPPDIK 552
Cdd:PHA03247 2726 AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASlsesresLPSPWDPA 2805

                         250
                  ....*....|.
gi 41053864   553 PNMSALPPPPA 563
Cdd:PHA03247 2806 DPPAAVLAPAA 2816
zf-Nse pfam11789
Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the ...
 744-790 9.97e-06

Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the fission yeast Smc5-6 DNA repair complex. This family is the zinc-finger domain similar to the MIZ type of zinc-finger.


Pssm-ID: 403098 [Multi-domain]  Cd Length: 57  Bit Score: 43.82  E-value: 9.97e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 41053864    744 KVSLKCPITFRRIQLPARGHDCKHVqcFDLESYLQLNCERGTWRCPV 790
Cdd:pfam11789    9 TISLTCPLTLQPFVEPVTSKKCNHV--FEKDAILEMLKRNPTVKCPV 53
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 322-552 1.16e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 49.69  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   322 SSFQMGPTQAYNSQFMNQPgPRGPASMGgsLNPAGMAAGMTPSGMSGPPMGMNQPR---PPGISPFGTHGQRmpqqtyPG 398
Cdd:PTZ00449  492 SKKKLAPIEEEDSDKHDEP-PEGPEASG--LPPKAPGDKEGEEGEHEDSKESDEPKeggKPGETKEGEVGKK------PG 562

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   399 P----RPQSLPIQSIKRPYPGEPNYGNQQYGPNS----QFPTQPGQYPTPNPPRPLTSPNYPgqRMPSQPSTGQYPPPtv 470
Cdd:PTZ00449  563 PakehKPSKIPTLSKKPEFPKDPKHPKDPEEPKKpkrpRSAQRPTRPKSPKLPELLDIPKSP--KRPESPKSPKRPPP-- 638

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   471 nmgqyykpeqfngqnntfssgssyssysqgsvnrPPRPVPvanyphspvPGNPTPPMTPGSSIPPYlSPsqdvKPPFPPD 550
Cdd:PTZ00449  639 ----------------------------------PQRPSS---------PERPEGPKIIKSPKPPK-SP----KPPFDPK 670


                  ..
gi 41053864   551 IK 552
Cdd:PTZ00449  671 FK 672
PHA03247 PHA03247
large tegument protein UL36; Provisional
 368-563 9.12e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 9.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   368 GPPmgmnQPRPPGISPFGTHGQRMPQQtyPGPRPQSLPIQS-IKRP-YPGEPNYGNQQYGPNSQFPTQPGQYPTP---NP 442
Cdd:PHA03247 2550 DPP----PPLPPAAPPAAPDRSVPPPR--PAPRPSEPAVTSrARRPdAPPQSARPRAPVDDRGDPRGPAPPSPLPpdtHA 2623

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   443 PRPLTSPNYPGQRMPSQPSTGQYPPPTVNMGQYYKPEQFNGQNNTFSSGSSYSSYSQGSVNRPPRPVPVANY-------P 515
Cdd:PHA03247 2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLtsladppP 2703

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 41053864   516 HSPVPGNPTPPMTPGSSIPPYLSPSQDVKPPFPPDIKPnmsalPPPPA 563
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAP-----PAVPA 2746
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 371-470 4.16e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 44.41  E-value: 4.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    371 MGMNQPrpPGISPF-GTHGQRM-----PQQTYPGpRPQSLPIQSiKRPYPGEPNYGNQ-----QYGPNSQFPTQPGQYPT 439
Cdd:TIGR01628  380 PRMRQL--PMGSPMgGAMGQPPyygqgPQQQFNG-QPLGWPRMS-MMPTPMGPGGPLRpnglaPMNAVRAPSRNAQNAAQ 455

                           90       100       110
                   ....*....|....*....|....*....|.
gi 41053864    440 PNPPRPLTSPnyPGQRMPSQPSTGQYPPPTV 470
Cdd:TIGR01628  456 KPPMQPVMYP--PNYQSLPLSQDLPQPQSTA 484
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 328-565 4.92e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.37  E-value: 4.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    328 PTQAYNSQFMNQPGPRGPASMGGSLNPAGMAAGMTPSGMSGPPMGMNQPRPPGISPFGTHGQRMPQ----QTYPGPRPQS 403
Cdd:pfam03154  213 ATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMphslQTGPSHMQHP 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    404 LPIQsikrPYPGEPNYGNQQY--GPNSQFPTQPGQYPTPNPPRPLTSPNYPGQRMPSQPSTGQY----PPPTVNMGQYYK 477
Cdd:pfam03154  293 VPPQ----PFPLTPQSSQSQVppGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMphikPPPTTPIPQLPN 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    478 PeqfngQNNTFSSGSSYSSYSQGSVNRPPRPV--PVANYPHSPVPGNPTPP---MTPGSSIPPylspsqdvkPPFPPDIK 552
Cdd:pfam03154  369 P-----QSHKHPPHLSGPSPFQMNSNLPPPPAlkPLSSLSTHHPPSAHPPPlqlMPQSQQLPP---------PPAQPPVL 434

                          250
                   ....*....|...
gi 41053864    553 PNMSALPPPPANH 565
Cdd:pfam03154  435 TQSQSLPPPAASH 447
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 386-541 7.64e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 43.26  E-value: 7.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    386 THGQRMPQQTYPGPRpqSLPIQSIKRPYPGEPNYGNQqyGPNSQFPTQPGQYPTpnpprpltSPNYPGQRMPSQPSTGQY 465
Cdd:TIGR01628  369 AHLQDQFMQLQPRMR--QLPMGSPMGGAMGQPPYYGQ--GPQQQFNGQPLGWPR--------MSMMPTPMGPGGPLRPNG 436

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    466 PPPTVNMGQYYKPEQfngqnntfssgssyssysqgsvNRPPRPvPVANYPHSP-------VPGNPTPPMTPGSSIPPYLS 538
Cdd:TIGR01628  437 LAPMNAVRAPSRNAQ----------------------NAAQKP-PMQPVMYPPnyqslplSQDLPQPQSTASQGGQNKKL 493


                   ...
gi 41053864    539 PSQ 541
Cdd:TIGR01628  494 AQV 496
PHA03369 PHA03369
capsid maturational protease; Provisional
 392-469 1.01e-03

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 43.06  E-value: 1.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053864   392 PQQTYPGPRPQSLPIQSIKRPYPGEPNYGNQQYGPNSQFPTQPGqyptpnpPRPLTSPNYPGQRMPSQPSTGQYPPPT 469
Cdd:PHA03369  371 APQTHTGPADRQRPQRPDGIPYSVPARSPMTAYPPVPQFCGDPG-------LVSPYNPQSPGTSYGPEPVGPVPPQPT 441
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 354-474 1.03e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 43.10  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    354 PAGMAAGMTPSGMSGPPMGMNQPRPPGISPFGTHGQRMPQQtyPGPRPQSLPIQSIKRP-----YPGEPNYGNQQYGPNS 428
Cdd:pfam09770  213 QPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQP--QQHPGQGHPVTILQRPqspqpDPAQPSIQPQAQQFHQ 290

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 41053864    429 QFPTQPGQyPT---PNPPRPLTSPnypgQRMPSQPSTGQYPPPTVNMGQ 474
Cdd:pfam09770  291 QPPPVPVQ-PTqilQNPNRLSAAR----VGYPQNPQPGVQPAPAHQAHR 334
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 319-541 1.21e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 43.07  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    319 PVCSSFQMGPTQAYNSQFMNQ----PGPRGPASMGGSLNPAGM-----AAGMTPSGMSGPPMGMNQPRPPGISPFGTHGQ 389
Cdd:pfam09606   81 DPINALQNLAGQGTRPQMMGPmgpgPGGPMGQQMGGPGTASNLlaslgRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQ 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    390 RMPQQTYPGPRPQSLPIQSIKRPYPGEPNYGnQQYGPNSQFPTQPGQyptPNPPRPLTSPNYPGQRMPsqpstGQYPPPT 469
Cdd:pfam09606  161 PSSGQPGSGTPNQMGPNGGPGQGQAGGMNGG-QQGPMGGQMPPQMGV---PGMPGPADAGAQMGQQAQ-----ANGGMNP 231

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41053864    470 VNMGQYYKPEQFNGQNNTFSSGSSYSSYSQGSVNRPPRPVPVANYPHSPVPGNPTPPMTPGsSIPPYLSPSQ 541
Cdd:pfam09606  232 QQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPG-AMPNVMSIGD 302
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 335-442 1.51e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.49  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    335 QFMnQPGPRGPASMGGSLNPAGMAA----GMTPSGMSGPPMGMNQPRPPGISPFGTHGQRMPQqTYPGPRPQSLPIQSiK 410
Cdd:TIGR01628  374 QFM-QLQPRMRQLPMGSPMGGAMGQppyyGQGPQQQFNGQPLGWPRMSMMPTPMGPGGPLRPN-GLAPMNAVRAPSRN-A 450

                           90       100       110
                   ....*....|....*....|....*....|..
gi 41053864    411 RPYPGEPNYGNQQYGPNSQFPTQPGQYPTPNP 442
Cdd:TIGR01628  451 QNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQS 482
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 506-583 2.00e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.10  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   506 PRPVPVANYPHSPVP----GNPTP---PMTPGSSIPPYLSPSQDVKPPFPPDIKPNMSALPPPPANHNDELRLTFPVRDG 578
Cdd:PRK14950  362 PVPAPQPAKPTAAAPspvrPTPAPstrPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVDEK 441


                  ....*
gi 41053864   579 VVLEP 583
Cdd:PRK14950  442 PKYTP 446
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 386-563 4.54e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.22  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   386 THGQRMPQQTYPGPRPQSL------PIQSIKRPYPGEPnygnqQYGPNSQFPTQPGQYPTPNPPRPLTSPNYPGQRMPSQ 459
Cdd:PRK10263  706 TQQQRYSGEQPAGANPFSLddfefsPMKALLDDGPHEP-----LFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQ 780

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   460 PSTGQYPPPtvnmgQYYKPEQfngqnntfssgSSYSSYSQGSVNRPPRPVPVANYPHSPV--------PGNPTPPMTPGS 531
Cdd:PRK10263  781 PQQPVAPQP-----QYQQPQQ-----------PVAPQPQYQQPQQPVAPQPQYQQPQQPVapqpqyqqPQQPVAPQPQDT 844

                         170       180       190
                  ....*....|....*....|....*....|...
gi 41053864   532 SIPPYLSPSQDVKPPFPPDIK-PNMSALPPPPA 563
Cdd:PRK10263  845 LLHPLLMRNGDSRPLHKPTTPlPSLDLLTPPPS 877
PHA03377 PHA03377
EBNA-3C; Provisional
 376-569 6.23e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 40.81  E-value: 6.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   376 PRPPGISPFGTHGQ-RMPQQTYPG---PRPQSLPIQSIKRPypgepnygNQQYGPNSQFPTQPGQYPT-PNPPRPLTS-- 448
Cdd:PHA03377  740 PPPSHQAPYSGHEEpQAQQAPYPGywePRPPQAPYLGYQEP--------QAQGVQVSSYPGYAGPWGLrAQHPRYRHSwa 811

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864   449 --PNYPGQRMPSQP--STGQYPPPTvnmgqyYKPEQFNGQNNTFSSGSSYSSYSqgsvnrPPRPvpvanyPHSPVPGNPT 524
Cdd:PHA03377  812 ywSQYPGHGHPQGPwaPRPPHLPPQ------WDGSAGHGQDQVSQFPHLQSETG------PPRL------QLSQVPQLPY 873

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 41053864   525 PPMTPGSSIPPYLSPsqdvkPPFPPdIKPNMSALPPPPANHNDEL 569
Cdd:PHA03377  874 SQTLVSSSAPSWSSP-----QPRAP-IRPIPTRFPPPPMPLQDSM 912
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 324-470 6.66e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 40.67  E-value: 6.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053864    324 FQMGPTQAYNSQFMNQPGPRGPASMGGSLNPAGMAAGMTPSGMSGPPMGMNQPRPPgiSPFGTHGQRMPQQTYPGPRPQS 403
Cdd:pfam05109  421 FSKAPESTTTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSP--TPAGTTSGASPVTPSPSPRDNG 498

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41053864    404 lpiQSIKRPYPGEPNYGNQQYGPNSQFPTQPGQYPTPNPPRPLTSPNYPGQRMPSQPSTGQYPPPTV 470
Cdd:pfam05109  499 ---TESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAV 562
 
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